Crystal Structure of Putidaredoxin, the [2Fe???2S] Component of the P450cam Monooxygenase System from Pseudomonas putida, Journal of Molecular Biology, vol.333, issue.2, pp.377-392, 2003. ,
DOI : 10.1016/j.jmb.2003.08.028
Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters, Proteins: Structure, Function, and Bioinformatics, vol.11, issue.5, pp.566-569, 2005. ,
DOI : 10.1002/prot.20481
Functional Assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-0RF3 Gene Cluster Involved in the Assembly of Fe-S Clusters in Escherichia coli, Journal of Biochemistry, vol.126, issue.5, pp.917-943, 1999. ,
DOI : 10.1093/oxfordjournals.jbchem.a022535
Bacterial ferredoxin, Bacteriol Rev, vol.28, pp.497-517, 1964. ,
Interplay of IscA and IscU in Biogenesis of Iron-Sulfur Clusters, Journal of Biological Chemistry, vol.281, issue.38, pp.27956-27963, 2006. ,
DOI : 10.1074/jbc.M601356200
Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis., Proceedings of the National Academy of Sciences, vol.90, issue.7, pp.2754-2758, 1993. ,
DOI : 10.1073/pnas.90.7.2754
Assembly of Iron-Sulfur Clusters: IDENTIFICATION OF AN iscSUA-hscBA-fdx GENE CLUSTER FROM AZOTOBACTER VINELANDII, Journal of Biological Chemistry, vol.273, issue.21, pp.13264-13272, 1998. ,
DOI : 10.1074/jbc.273.21.13264
Structure, function and evolution of bacterial ferredoxins, FEMS Microbiology Letters, vol.54, issue.2, pp.155-176, 1988. ,
DOI : 10.1111/j.1574-6968.1988.tb02741.x
URL : https://hal.archives-ouvertes.fr/hal-00320314
Vertebrate-type and plant-type ferredoxins: crystal structure comparison and electron transfer pathway modelling, Journal of Molecular Biology, vol.294, issue.2, pp.501-513, 1999. ,
DOI : 10.1006/jmbi.1999.3253
Cytochrome P450: Structure, function, and generation of reactive oxygen species, Rev Physiol Biochem Pharmacol, vol.127, pp.137-221, 1996. ,
DOI : 10.1007/BFb0048267
Electron Transport in Cytochromes P-450 by Covalent Switching, Proceedings of the Royal Society B: Biological Sciences, vol.245, issue.1312, pp.43-51, 1991. ,
DOI : 10.1098/rspb.1991.0086
Functional Assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-0RF3 Gene Cluster Involved in the Assembly of Fe-S Clusters in Escherichia coli, Journal of Biochemistry, vol.126, issue.5, pp.917-926, 1999. ,
DOI : 10.1093/oxfordjournals.jbchem.a022535
A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins, Proceedings of the National Academy of Sciences, vol.97, issue.3, pp.1050-1055, 2000. ,
DOI : 10.1073/pnas.97.3.1050
Adrenodoxin: Structure, stability, and electron transfer properties, Proteins: Structure, Function, and Genetics, vol.11, issue.4, pp.590-612, 2000. ,
DOI : 10.1002/1097-0134(20000901)40:4<590::AID-PROT50>3.0.CO;2-P
Crystal Structure of Putidaredoxin, the [2Fe???2S] Component of the P450cam Monooxygenase System from Pseudomonas putida, Journal of Molecular Biology, vol.333, issue.2, pp.377-392, 2003. ,
DOI : 10.1016/j.jmb.2003.08.028
and characterization of its product, a [2Fe-2S] ferredoxin, Biochemical Journal, vol.300, issue.2, pp.413-418, 1994. ,
DOI : 10.1042/bj3000413
Purification of a sixth ferredoxin from Rhodobacter capsulatus. Primary structure and biochemical properties, European Journal of Biochemistry, vol.133, issue.3, pp.933-939, 1994. ,
DOI : 10.1007/BF00279903
A [2Fe-2S] ferredoxin (FdVI) is essential for growth of the photosynthetic bacterium Rhodobacter capsulatus., Journal of Bacteriology, vol.179, issue.10, pp.3304-3309, 1997. ,
DOI : 10.1128/jb.179.10.3304-3309.1997
A microspectrophotometer for UV???visible absorption and fluorescence studies of protein crystals, Journal of Applied Crystallography, vol.35, issue.3, pp.319-326, 2002. ,
DOI : 10.1107/S0021889802003837
A theoretical interpretation of the variations of some physical parameters within the [2Fe-2S] ferredoxin group, Biochimica et Biophysica Acta (BBA) - Protein Structure, vol.579, issue.1, pp.107-121, 1979. ,
DOI : 10.1016/0005-2795(79)90091-6
: a program for deriving anomalous-scattering factors from X-ray fluorescence spectra, Journal of Applied Crystallography, vol.34, issue.1, pp.82-86, 2001. ,
DOI : 10.1107/S0021889800014655
[17] Charge-coupled device-based area detectors, Methods Enzymol, vol.276, pp.244-268, 1997. ,
DOI : 10.1016/S0076-6879(97)76063-4
Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallographica Section A Foundations of Crystallography, vol.47, issue.2, pp.110-119, 1991. ,
DOI : 10.1107/S0108767390010224
: an automated package for molecular replacement, Acta Crystallographica Section A Foundations of Crystallography, vol.50, issue.2, pp.157-163, 1994. ,
DOI : 10.1107/S0108767393007597
STRING: a database of predicted functional associations between proteins, Nucleic Acids Research, vol.31, issue.1, pp.258-261, 2003. ,
DOI : 10.1093/nar/gkg034
Purification and Biophysical Characterization of a New [2Fe-2S] Ferredoxin from Azotobacter vinelandii, a Putative [Fe-S] Cluster Assembly/Repair Protein, Journal of Biological Chemistry, vol.274, issue.45, pp.32402-32410, 1999. ,
DOI : 10.1074/jbc.274.45.32402
Expression of Maize Ferredoxin cDNA in Escherichia coli : Comparison of Photosynthetic and Nonphotosynthetic Ferredoxin Isoproteins and their Chimeric Molecule, PLANT PHYSIOLOGY, vol.97, issue.4, pp.1395-1401, 1991. ,
DOI : 10.1104/pp.97.4.1395
Redox thermodynamics of low-potential iron-sulfur proteins, JBIC Journal of Biological Inorganic Chemistry, vol.5, issue.6, pp.748-760, 2000. ,
DOI : 10.1007/s007750000164
Reduction potential and thermodynamic parameters of adrenodoxin by the use of an anaerobic thin-layer electrode, Analytical Biochemistry, vol.133, issue.2, pp.385-393, 1983. ,
DOI : 10.1016/0003-2697(83)90099-4
Conformational stability of adrenodoxin mutant proteins, Protein Science, vol.12, issue.9, pp.1890-1897, 1996. ,
DOI : 10.1002/pro.5560050915
Probing the Interactions of Putidaredoxin with Redox Partners in Camphor P450 5-Monooxygenase by Mutagenesis of Surface Residues, Journal of Biological Chemistry, vol.272, issue.35, pp.21720-21725, 1997. ,
DOI : 10.1074/jbc.272.35.21720
Redox-dependent Structural Reorganization in Putidaredoxin, a Vertebrate-type [2Fe-2S] Ferredoxin from Pseudomonas putida, Journal of Molecular Biology, vol.347, issue.3, pp.607-628, 2005. ,
DOI : 10.1016/j.jmb.2005.01.047
Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons, Proteins: Structure, Function, and Genetics, vol.39, issue.4, pp.281-296, 1991. ,
DOI : 10.1002/prot.340110407
and characterization of its product, a [2Fe-2S] ferredoxin, Biochemical Journal, vol.300, issue.2, pp.413-418, 1994. ,
DOI : 10.1042/bj3000413
A [2Fe-2S] ferredoxin (FdVI) is essential for growth of the photosynthetic bacterium Rhodobacter capsulatus., Journal of Bacteriology, vol.179, issue.10, pp.3304-3309, 1997. ,
DOI : 10.1128/jb.179.10.3304-3309.1997
Atomically defined mechanism for proton transfer to a buried redox centre in a protein, Nature, vol.405, issue.6788, pp.814-817, 2000. ,
DOI : 10.1038/35015610
Transcriptional analysis and promoter mapping of the fdxA gene which encodes the 7Fe ferredoxin (FdII) of Rhodobacter capsulatus, Mol. Gen. Genet, vol.231, pp.323-328, 1992. ,
A new [2Fe-2S] ferredoxin from Rhodobacter capsulatus. Coexpression with a 2[4Fe-4S] ferredoxin in Escherichia coli, J. Biol. Chem, vol.266, pp.3294-3299, 1991. ,
Purification and characterization of a 7Fe-ferredoxin from Rhodobacter capsulatus, Biochemical and Biophysical Research Communications, vol.171, issue.1, pp.273-279, 1990. ,
DOI : 10.1016/0006-291X(90)91388-9
Purification and Biophysical Characterization of a New [2Fe-2S] Ferredoxin from Azotobacter vinelandii, a Putative [Fe-S] Cluster Assembly/Repair Protein, Journal of Biological Chemistry, vol.274, issue.45, pp.32402-32410, 1999. ,
DOI : 10.1074/jbc.274.45.32402
Redox-dependent Structural Reorganization in Putidaredoxin, a Vertebrate-type [2Fe-2S] Ferredoxin from Pseudomonas putida, Journal of Molecular Biology, vol.347, issue.3, pp.607-621, 2005. ,
DOI : 10.1016/j.jmb.2005.01.047
Crystal Structure of the Terminal Oxygenase Component of Cumene Dioxygenase from Pseudomonas fluorescens IP01, Journal of Bacteriology, vol.187, issue.7, pp.2483-2490, 2005. ,
DOI : 10.1128/JB.187.7.2483-2490.2005
Use of surfactants to enhance the removal of PAHs from soil, Polycyclic Aromatic Compounds, vol.20, pp.143-154, 2000. ,
The University of Minnesota Biocatalysis/Biodegradation Database: the first decade, Nucleic Acids Research, vol.34, issue.90001, pp.517-521, 2006. ,
DOI : 10.1093/nar/gkj076
Rieske business: Structure???function of Rieske non-heme oxygenases, Biochemical and Biophysical Research Communications, vol.338, issue.1, pp.175-190, 2005. ,
DOI : 10.1016/j.bbrc.2005.08.222
Structural Insight into the Dioxygenation of Nitroarene Compounds: the Crystal Structure of Nitrobenzene Dioxygenase, Journal of Molecular Biology, vol.348, issue.5, pp.1139-1151, 2005. ,
DOI : 10.1016/j.jmb.2005.03.052
Biphenyl Dioxygenases: Functional Versatilities and Directed Evolution, Journal of Bacteriology, vol.186, issue.16, pp.5189-5196, 2004. ,
DOI : 10.1128/JB.186.16.5189-5196.2004
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC490896
Crystal Structure of the Terminal Oxygenase Component of Biphenyl Dioxygenase Derived from Rhodococcus sp. Strain RHA1, Journal of Molecular Biology, vol.342, issue.3, pp.1041-1052, 2004. ,
DOI : 10.1016/j.jmb.2004.07.062
Oxidation of the carcinogens benzo [a] pyrene and benzo [a] anthracene to dihydrodiols by a bacterium, Science, vol.189, issue.4199, pp.295-297, 1975. ,
DOI : 10.1126/science.1145203
Characterization of Hybrid Toluate and Benzoate Dioxygenases, Journal of Bacteriology, vol.185, issue.18, pp.5333-5341, 2003. ,
DOI : 10.1128/JB.185.18.5333-5341.2003
Beijerinckia sp strain B1: a strain by any other name . . . . ., Journal of Industrial Microbiology and Biotechnology, vol.23, issue.4-5, pp.284-293, 1999. ,
DOI : 10.1038/sj.jim.2900715
Composting for soil remediation In Biological treatment of hazardous wastes, pp.373-395, 1997. ,
Cis-1,2-dihydroxy-1,2-dihydronaphthalene: A bacterial metabolite from naphthalene, Archives of Biochemistry and Biophysics, vol.142, issue.1, pp.394-396, 1971. ,
DOI : 10.1016/0003-9861(71)90298-0
Principles of microbial PAH-degradation in soil, Environmental Pollution, vol.133, issue.1, pp.71-84, 2005. ,
DOI : 10.1016/j.envpol.2004.04.015
Solvent-Augmented Mineralization of Pyrene by a Mycobacterium sp, Appl. Environ. Microbiol, vol.62, pp.2311-2316, 1996. ,
Increases in the polynuclear aromatic hydrocarbon content of an agricultural soil over the last century, Environmental Science & Technology, vol.23, issue.1, pp.95-101, 1989. ,
DOI : 10.1021/es00178a012
Stimulation of Pyrene Mineralization in Freshwater Sediments by Bacterial and Plant Bioaugmentation, Environmental Science & Technology, vol.39, issue.15, pp.5729-5735, 2005. ,
DOI : 10.1021/es050412d
URL : https://hal.archives-ouvertes.fr/halsde-00294538
Degradation of fluoranthene, pyrene, benz[a]anthracene and dibenz[a,h]anthracene by Burkholderia cepacia, Journal of Applied Microbiology, vol.83, issue.2, pp.189-198, 1997. ,
DOI : 10.1046/j.1365-2672.1997.00220.x
Biodegradation of High-Molecular-Weight Polycyclic Aromatic Hydrocarbons by Bacteria, Journal of Bacteriology, vol.182, issue.8, pp.2059-2067, 2000. ,
DOI : 10.1128/JB.182.8.2059-2067.2000
Rapid Mineralization of Benzo[a]pyrene by a Microbial Consortium Growing on Diesel Fuel, Applied and Environmental Microbiology, vol.66, issue.10, pp.4205-4211, 2000. ,
DOI : 10.1128/AEM.66.10.4205-4211.2000
X-ray Crystal Structure of Benzoate 1,2-Dioxygenase Reductase from Acinetobacter sp. Strain ADP1, Journal of Molecular Biology, vol.318, issue.2, pp.261-272, 2002. ,
DOI : 10.1016/S0022-2836(02)00039-6
Enumeration and characterization of the soil microflora from hydrocarbon-contaminated soil sites able to mineralize polycyclic aromatic hydrocarbons (PAH), Applied Microbiology and Biotechnology, vol.41, issue.2, pp.267-273, 1994. ,
DOI : 10.1007/BF00186971
Functional analyses of a variety of chimeric dioxygenases constructed from two biphenyl dioxygenases that are similar structurally but different functionally., Journal of Bacteriology, vol.179, issue.12, pp.3936-3943, 1997. ,
DOI : 10.1128/jb.179.12.3936-3943.1997
Benzene-Induced Uncoupling of Naphthalene Dioxygenase Activity and Enzyme Inactivation by Production of Hydrogen Peroxide, J. Bacteriol, vol.181, pp.719-2725, 1999. ,
New Classification System for Oxygenase Components Involved in Ring-Hydroxylating Oxygenations, Bioscience, Biotechnology, and Biochemistry, vol.180, issue.15, pp.254-263, 2001. ,
DOI : 10.1016/S0922-338X(97)80347-9
Metabolism of phenanthrene by the marine cyanobacterium Agmenellum quadruplicatum PR-6, Appl. Environ. Microbiol, vol.58, pp.1351-1359, 1992. ,
Structure of the terminal oxygenase component of angular dioxygenase, J. Mol. Biol, vol.1, issue.351, pp.9-355, 2005. ,
Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity, J. Bacteriol, vol.181, pp.1831-1837, 1999. ,
Substrate Specificity of Naphthalene Dioxygenase: Effect of Specific Amino Acids at the Active Site of the Enzyme, Journal of Bacteriology, vol.182, issue.6, pp.1641-1649, 2000. ,
DOI : 10.1128/JB.182.6.1641-1649.2000
PAH dissipation in a contaminated river sediment under oxic and anoxic conditions, Environmental Pollution, vol.134, issue.2, pp.315-322, 2005. ,
DOI : 10.1016/j.envpol.2004.07.022
URL : https://hal.archives-ouvertes.fr/hal-00379875
Genotoxicity of complex PAH mixtures recovered from contaminated lake sediments as assessed by three different methods, Environmental and Molecular Mutagenesis, vol.120, issue.4, pp.303-312, 1999. ,
DOI : 10.1002/(SICI)1098-2280(1999)33:4<303::AID-EM7>3.0.CO;2-0
Degradation of pyrene, benz[a]anthracene, and benzo[a]pyrene by Mycobacterium sp. strain RJGII-135, isolated from a former coal gasification site, Appl. Environ. Microbiol, vol.62, pp.13-19, 1996. ,
Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase, Journal of Molecular Biology, vol.304, issue.3, pp.397-410, 2000. ,
DOI : 10.1006/jmbi.2000.4200
DNA Adduct Formation by Polycyclic Aromatic Hydrocarbon Dihydrodiol Epoxides, Chemical Research in Toxicology, vol.11, issue.1, pp.1-11, 1998. ,
DOI : 10.1021/tx970142f
Isolation and characterization of a novel sphingomonad capable of growth with chrysene as sole carbon and energy source, FEMS Microbiology Letters, vol.241, issue.2, pp.143-150, 2004. ,
DOI : 10.1016/j.femsle.2004.10.012
Degradation of pyrene byRhodococcus sp. UW1, Applied Microbiology and Biotechnology, vol.4, issue.5, pp.671-676, 1991. ,
DOI : 10.1007/BF00167921
The Broad Substrate Chlorobenzene Dioxygenase and cis-Chlorobenzene Dihydrodiol Dehydrogenase of Pseudomonas sp. Strain P51 Are Linked Evolutionarily to the Enzymes for Benzene and Toluene Degradation, J. Biol. Chem, vol.271, pp.4009-4016, 1996. ,
Single Turnover Chemistry and Regulation of O2Activation by the Oxygenase Component of Naphthalene 1,2-Dioxygenase, Journal of Biological Chemistry, vol.276, issue.3, pp.1945-1953, 2001. ,
DOI : 10.1074/jbc.M007795200
Hydrogen Peroxide-coupled cis-Diol Formation Catalyzed by Naphthalene 1,2-Dioxygenase, Journal of Biological Chemistry, vol.278, issue.2, pp.829-835, 2003. ,
DOI : 10.1074/jbc.M209604200
Genetics of Naphthalene Catabolism in Pseudomonads, CRC Critical Reviews in Microbiology, vol.237, issue.3, pp.247-268, 1988. ,
DOI : 10.3109/10408448509037460
Structure-function Analysis of the Bacterial Aromatic Ring-hydroxylating Dioxygenases, References Adv. Microb. Physiol, vol.38, issue.1, pp.47-84, 1997. ,
DOI : 10.1016/S0065-2911(08)60155-1
Aromatic hydrocarbon dioxygenases in environmental biotechnology, Current Opinion in Biotechnology, vol.11, issue.3, pp.236-243, 2000. ,
DOI : 10.1016/S0958-1669(00)00090-2
Genetic analysis of dioxin dioxygenase of Sphingomonas sp. Strain RW1: catabolic genes dispersed on the genome, J. Bacteriol, vol.180, issue.3, pp.3954-3966, 1998. ,
Dibenzofuran 4,4a-dioxygenase from Sphingomonas sp. strain RW1: angular dioxygenation by a three-component enzyme system., Journal of Bacteriology, vol.175, issue.20, pp.6467-6475, 1993. ,
DOI : 10.1128/jb.175.20.6467-6475.1993
Biphenyl Dioxygenases: Functional Versatilities and Directed Evolution, Journal of Bacteriology, vol.186, issue.16, pp.5189-5196, 2004. ,
DOI : 10.1128/JB.186.16.5189-5196.2004
Identification and Functional Analysis of Two Aromatic-Ring-Hydroxylating Dioxygenases from a Sphingomonas Strain That Degrades Various Polycyclic Aromatic Hydrocarbons, Applied and Environmental Microbiology, vol.70, issue.11, pp.6714-6725, 2004. ,
DOI : 10.1128/AEM.70.11.6714-6725.2004
Identification of Pyrene-Induced Proteins in Mycobacterium sp. Strain 6PY1: Evidence for Two Ring-Hydroxylating Dioxygenases, Journal of Bacteriology, vol.185, issue.13, pp.3828-3841, 2003. ,
DOI : 10.1128/JB.185.13.3828-3841.2003
URL : https://hal.archives-ouvertes.fr/halsde-00295028
A novel phenanthrene dioxygenase from Nocardioides sp strain KP7: Expression in Escherichia coli Engineering dioxygenases for efficient degradation of environmental pollutants, J. Bacteriol. Curr. Opin. Biotechnol, vol.182, issue.11, pp.2134-2141, 2000. ,
Single Turnover Chemistry and Regulation of O2Activation by the Oxygenase Component of Naphthalene 1,2-Dioxygenase, Journal of Biological Chemistry, vol.276, issue.3, pp.1945-1953, 2001. ,
DOI : 10.1074/jbc.M007795200
Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia, J. Biol. Chem, vol.262, issue.11, pp.1510-1518, 1987. ,
Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S], Science, vol.258, issue.5088, pp.1604-1610, 1992. ,
DOI : 10.1126/science.1280857
Structure of an aromatic-ring-hydroxylating dioxygenase ??? naphthalene 1,2-dioxygenase, Structure, vol.6, issue.5, pp.571-586, 1998. ,
DOI : 10.1016/S0969-2126(98)00059-8
Substrate Specificity of Naphthalene Dioxygenase: Effect of Specific Amino Acids at the Active Site of the Enzyme, Journal of Bacteriology, vol.182, issue.6, pp.1641-1649, 2000. ,
DOI : 10.1128/JB.182.6.1641-1649.2000
Bacterial oxidation of chemical carcinogens: formation of polycyclic aromatic acids from benz[a]anthracene, Appl. Environ. Microbiol, vol.54, pp.2415-2423, 1988. ,
-Dihydroxylation of Polycyclic Arenes and Heteroarenes, The Journal of Organic Chemistry, vol.64, issue.11, pp.4005-4011, 1999. ,
DOI : 10.1021/jo982517n
URL : https://hal.archives-ouvertes.fr/in2p3-00025581
Bioremediation of high molecular weight polycyclic aromatic hydrocarbons: a review of the microbial degradation of benzo[a]pyrene, International Biodeterioration & Biodegradation, vol.45, issue.1-2, pp.45-57, 2000. ,
DOI : 10.1016/S0964-8305(00)00052-4
Biodegradation of High-Molecular-Weight Polycyclic Aromatic Hydrocarbons by Bacteria, Journal of Bacteriology, vol.182, issue.8, pp.2059-2067, 2000. ,
DOI : 10.1128/JB.182.8.2059-2067.2000
Oxidation of the carcinogens benzo [a] pyrene and benzo [a] anthracene to dihydrodiols by a bacterium, Science, vol.189, issue.4199, pp.295-297, 1975. ,
DOI : 10.1126/science.1145203
Degradation of pyrene by Mycobacterium flavescens, Applied Microbiology and Biotechnology, vol.46, issue.3, pp.307-312, 1996. ,
DOI : 10.1007/s002530050822
Bacterial dioxygenase-catalysed dihydroxylation and chemical resolution routes to enantiopure cis-dihydrodiols of chrysene, J. Chem. Soc. Perkin Trans. 1, pp.1715-1723, 1997. ,
Identification of Pyrene-Induced Proteins in Mycobacterium sp. Strain 6PY1: Evidence for Two Ring-Hydroxylating Dioxygenases, Journal of Bacteriology, vol.185, issue.13, pp.185-3828, 2003. ,
DOI : 10.1128/JB.185.13.3828-3841.2003
URL : https://hal.archives-ouvertes.fr/halsde-00295028
Isolation and characterization of a novel sphingomonad capable of growth with chrysene as sole carbon and energy source, FEMS Microbiology Letters, vol.241, issue.2, pp.143-150, 2004. ,
DOI : 10.1016/j.femsle.2004.10.012
Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Spingomonas strain that degrades variuous polycyclic aromatic hydrocarbons, App. Environment. Microbiol, pp.70-6714, 2004. ,
The Broad Substrate Chlorobenzene Dioxygenase and cis-Chlorobenzene Dihydrodiol Dehydrogenase of Pseudomonas sp. Strain P51 Are Linked Evolutionarily to the Enzymes for Benzene and Toluene Degradation, J. Biol. Chem, pp.271-4009, 1996. ,
Structure of an aromatic-ring-hydroxylating dioxygenase ??? naphthalene 1,2-dioxygenase, Structure, vol.6, issue.5, pp.2-571, 1998. ,
DOI : 10.1016/S0969-2126(98)00059-8
Substrate binding site of naphthalene 1,2-dioxygenase: functional implications of indole binding, Journal of Molecular Biology, vol.296, issue.2, pp.296-701, 2000. ,
DOI : 10.1006/jmbi.1999.3462
Crystal Structure of Naphthalene Dioxygenase: Side-on Binding of Dioxygen to Iron, Crystal Structure of Naphthalene Dioxygenase: Side-on binding of Dioxygen to Iron, pp.1039-1042, 2003. ,
DOI : 10.1126/science.1078020
Structure and Increased Thermostability of Rhodococcus sp, Naphthalene J.Bacteriol, vol.1, issue.187, pp.2-7222, 2005. ,
Structural insight into the dioxygenation of nitroarene compounds: the crystal structure of nitrobenzene dioxygenase, J. Mol. Biol, vol.348, pp.1139-1151, 2005. ,
Crystal Structure of the Terminal Oxygenase Component of Biphenyl Dioxygenase Derived from Rhodococcus sp. Strain RHA1, Journal of Molecular Biology, vol.342, issue.3, pp.342-1041, 2004. ,
DOI : 10.1016/j.jmb.2004.07.062
Crystal Structure of the Terminal Oxygenase Component of Cumene Dioxygenase from Pseudomonas fluorescens IP01, Journal of Bacteriology, vol.187, issue.7, pp.2483-2490, 2005. ,
DOI : 10.1128/JB.187.7.2483-2490.2005
2-Oxoquinoline 8-Monooxygenase Oxygenase Component: Active Site Modulation by Rieske-[2Fe-2S] Center Oxidation/Reduction, Structure, vol.13, issue.5, pp.817-824, 2005. ,
DOI : 10.1016/j.str.2005.03.008
Structure of the terminal oxygenase component of angular dioxygenase, carbazole 1,9a-dioxygenase, J. Mol. Biol, pp.351-355, 2005. ,
Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites, Chemical Reviews, vol.96, issue.7, pp.2607-2624, 1996. ,
DOI : 10.1021/cr960039f
Comparative Studies of Protein Crystallization by Vapour-Diffusion and Microbatch Techniques, Acta Crystallographica Section D Biological Crystallography, vol.54, issue.1, pp.8-15, 1998. ,
DOI : 10.1107/S0907444997005374
A Modular Approach to Beam Line Automation: The NIGMS Facility at the NSLS, pp.20-25, 2003. ,
[20] Processing of X-ray diffraction data collected in oscillation mode, Methods in Enzymology, vol.276, pp.307-326, 1997. ,
DOI : 10.1016/S0076-6879(97)76066-X
: an Automated Program for Molecular Replacement, Journal of Applied Crystallography, vol.30, issue.6 ,
DOI : 10.1107/S0021889897006766
An automated procedure for phase improvement by density modification, Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography, vol.31, pp.34-38, 1994. ,
Solvent content of protein crystals, Journal of Molecular Biology, vol.33, issue.2, pp.491-497, 1968. ,
DOI : 10.1016/0022-2836(68)90205-2
Automated protein model building combined with iterative structure refinement, Nature Structural Biology, vol.6, issue.5, pp.458-463, 1999. ,
DOI : 10.1038/8263
: model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.60-2126, 2004. ,
DOI : 10.1107/S0907444904019158
Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.53-240, 1997. ,
DOI : 10.1107/S0907444996012255
PROCHECK: a program to check the stereochemical quality of protein structures, Journal of Applied Crystallography, vol.26, issue.2, pp.26-283, 1993. ,
DOI : 10.1107/S0021889892009944
Functional and Evolutionary Relationships Among Diverse Oxygenases, Annual Review of Microbiology, vol.46, issue.1, pp.565-601, 1992. ,
DOI : 10.1146/annurev.mi.46.100192.003025
Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity, J. Bacteriol, pp.181-1831, 1999. ,
A theoretical study of the cis-dihydroxylation mechanism in naphthalene 1,2-dioxygenase, J. Biol. Inorg. Chem, vol.9, pp.439-52, 2004. ,
Substrate Specificity of Naphthalene Dioxygenase: Effect of Specific Amino Acids at the Active Site of the Enzyme, Journal of Bacteriology, vol.182, issue.6, pp.182-1641, 2000. ,
DOI : 10.1128/JB.182.6.1641-1649.2000
improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res, vol.22, pp.4673-4680, 1994. ,
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, Journal of Applied Crystallography, vol.24, issue.5, pp.946-950, 1991. ,
DOI : 10.1107/S0021889891004399
Raster3D Version 2.0. A program for photorealistic molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.50, issue.6, pp.50-869, 1994. ,
DOI : 10.1107/S0907444994006396
Structure-function Analysis of the Bacterial Aromatic Ring-hydroxylating Dioxygenases, Adv. Microb. Physiol, vol.38, pp.47-84, 1997. ,
DOI : 10.1016/S0065-2911(08)60155-1
Bioremediation of high molecular weight polycyclic aromatic hydrocarbons: a review of the microbial degradation of benzo[a]pyrene, International Biodeterioration & Biodegradation, vol.45, issue.1-2, pp.57-88, 2000. ,
DOI : 10.1016/S0964-8305(00)00052-4
Biodegradation of High-Molecular-Weight Polycyclic Aromatic Hydrocarbons by Bacteria, Journal of Bacteriology, vol.182, issue.8, pp.2059-2067, 2000. ,
DOI : 10.1128/JB.182.8.2059-2067.2000
Identification and Functional Analysis of Two Aromatic-Ring-Hydroxylating Dioxygenases from a Sphingomonas Strain That Degrades Various Polycyclic Aromatic Hydrocarbons, Applied and Environmental Microbiology, vol.70, issue.11, pp.70-6714, 2004. ,
DOI : 10.1128/AEM.70.11.6714-6725.2004
Structure of an aromatic-ring-hydroxylating dioxygenase ??? naphthalene 1,2-dioxygenase, Structure, vol.6, issue.5, pp.2-571, 1998. ,
DOI : 10.1016/S0969-2126(98)00059-8
Structure and Increased Thermostability of Rhodococcus sp, Naphthalene J. Bacteriol, vol.1, issue.197, pp.2-7222, 2005. ,
Rieske business: Structure???function of Rieske non-heme oxygenases, Biochemical and Biophysical Research Communications, vol.338, issue.1, pp.175-190, 2005. ,
DOI : 10.1016/j.bbrc.2005.08.222
A novel technique to control the rate of vapour diffusion, giving larger protein crystals, Journal of Applied Crystallography, vol.30, issue.2, pp.198-202, 1997. ,
DOI : 10.1107/S0021889896013532
Crystal Structure of the Terminal Oxygenase Component of Cumene Dioxygenase from Pseudomonas fluorescens IP01, Journal of Bacteriology, vol.187, issue.7, pp.2483-2490, 2005. ,
DOI : 10.1128/JB.187.7.2483-2490.2005
Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.53-240, 1997. ,
DOI : 10.1107/S0907444996012255
: model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.60-2126, 2004. ,
DOI : 10.1107/S0907444904019158
Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design, Protein Science, vol.245, issue.9, pp.1884-1897, 1998. ,
DOI : 10.1002/pro.5560070905
2-Oxoquinoline 8-Monooxygenase Oxygenase Component: Active Site Modulation by Rieske-[2Fe-2S] Center Oxidation/Reduction, Structure, vol.13, issue.5, pp.817-824, 2005. ,
DOI : 10.1016/j.str.2005.03.008
Structure of the terminal oxygenase component of angular dioxygenase, carbazole 1,9a-dioxygenase, J. Mol. Biol, pp.351-355, 2005. ,
New Classification System for Oxygenase Components Involved in Ring-Hydroxylating Oxygenations, New Classification System for Oxygenase Components Involved in Ring-Hydroxylating Oxygenations, pp.254-263, 2001. ,
DOI : 10.1016/S0922-338X(97)80347-9
The role of active-site residues in naphthalene dioxygenase, Journal of Industrial Microbiology and Biotechnology, vol.30, issue.5, pp.271-278, 2003. ,
DOI : 10.1007/s10295-003-0043-3
Regioselectivity and Enantioselectivity of Naphthalene Dioxygenase during Arene cis-Dihydroxylation: Control by Phenylalanine 352 in the alpha Subunit, Journal of Bacteriology, vol.182, issue.19, pp.182-5495, 2000. ,
DOI : 10.1128/JB.182.19.5495-5504.2000
Structural Insight Into the Dioxygenation of Nitroarene Compounds: The Crystal Structure of Nitrobenzene Dioxygenase, J. Mol. Biol, vol.348, pp.1139-1151, 2005. ,
An extensively modified version of MolScript that includes greatly enhanced coloring capabilities, Journal of Molecular Graphics and Modelling, vol.15, issue.2, pp.132-134, 1997. ,
DOI : 10.1016/S1093-3263(97)00021-1
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, Journal of Applied Crystallography, vol.24, issue.5, pp.946-950, 1991. ,
DOI : 10.1107/S0021889891004399
Raster3D Version 2.0. A program for photorealistic molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.50, issue.6, pp.50-869, 1994. ,
DOI : 10.1107/S0907444994006396
software for automated crystallographic structure determination, Journal of Synchrotron Radiation, vol.11, issue.1, pp.53-55, 2004. ,
DOI : 10.1107/S0909049503024130
One-and-a-half wavelength approach, Acta Crystallographica Section D Biological Crystallography, vol.58, issue.11, pp.1958-1967, 2002. ,
DOI : 10.1107/S0907444902016645
Cryo-Protection of Protein Crystals against Radiation Damage in Electron and X-Ray Diffraction, Proc. R. Soc. London. B241, pp.6-8, 1990. ,
DOI : 10.1098/rspb.1990.0057
Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur, Nature, vol.206, issue.5802, pp.107-113, 1981. ,
DOI : 10.1038/290107a0
Selenomethionyl proteins produced for analysis by Multiwavelength Anomalous Diffraction (MAD): a vehicle for direct determination of three-dimensional structure, EMBO J, vol.9, pp.1665-1672, 1990. ,
Radiation damage in protein crystals at low temperature, Acta Crystallographica Section D Biological Crystallography, vol.50, issue.6, 1994. ,
DOI : 10.1107/S0907444994006311
Automation of the collection and processing of X-ray diffraction data ??? a generic approach, Acta Crystallographica Section D Biological Crystallography, vol.58, issue.11, pp.1924-1928, 2002. ,
DOI : 10.1107/S0907444902016864
High Throughput Macromolecular Crystallization for Structural Genomics, Proceedings of NATO ASI 30th Course -Methods in Macromolecular Crystallography, "Ettore Majorana" Centre for Scientific Culture, 2000. ,
Investigation of possible free-radical scavengers and metrics for radiation damage in protein cryocrystallography, Journal of Synchrotron Radiation, vol.9, issue.6, pp.347-354, 2002. ,
DOI : 10.1107/S0909049502014632
X-ray absorption by macromolecular crystals: the effects of wavelength and crystal composition on absorbed dose, Journal of Applied Crystallography, vol.37, issue.4, pp.513-522, 2004. ,
DOI : 10.1107/S0021889804010660
Phasing Macromolecular Structures with UV-Induced Structural Changes, Structure, vol.14, issue.4, pp.791-800, 2006. ,
DOI : 10.1016/j.str.2006.02.007
Physical and chemical considerations of damage induced in protein crystals by synchrotron radiation: a radiation chemical perspective, Journal of Synchrotron Radiation, vol.9, issue.6, pp.329-332, 2002. ,
DOI : 10.1107/S0909049502014553
Phasing on anomalous signal of sulfurs: what is the limit?, Acta Crystallographica Section D Biological Crystallography, vol.59, issue.6, pp.1020-1027, 2003. ,
DOI : 10.1107/S0907444903007467
Single-wavelength anomalous diffraction phasing revisited, Acta Crystallographica Section D Biological Crystallography, vol.56, issue.11, pp.1413-1420, 2000. ,
DOI : 10.1107/S0907444900010039
XOP: Recent developments, SPIE proceedings, vol.3448, 1998. ,
How does radiation damage in protein crystals depend on X-ray dose? Structure, pp.13-19, 2003. ,
Primary radiation damage of protein crystals by an intense synchrotron X-ray beam, Journal of Synchrotron Radiation, vol.7, issue.5, pp.313-317, 2000. ,
DOI : 10.1107/S0909049500008694
On the influence of the incident photon energy on the radiation damage in crystalline biological samples, Journal of Synchrotron Radiation, vol.12, issue.3, pp.304-309, 2005. ,
DOI : 10.1107/S0909049505003328
Specific Chemical and Structural Damage to Proteins Produce by Synchrotron Radiation, Proc. Nat. Acad. Sci. USA, pp.623-628, 2000. ,
Away from the edge: SAD phasing from the sulfur anomalous signal measured in-house with chromium radiation, Acta Crystallographica Section D Biological Crystallography, vol.59, issue.11, 2003. ,
DOI : 10.1107/S0907444903018547
Optimum X-ray wavelength for protein crystallography, Journal of Applied Crystallography, vol.17, issue.2, pp.118-119, 1984. ,
DOI : 10.1107/S0021889884011092
Acta Cryst, pp.1085-1093, 2004. ,
EF-hands at atomic resolution: the structure of human psoriasin (S100A7) solved by MAD phasing, Structure, vol.6, issue.4, pp.477-489, 1998. ,
DOI : 10.1016/S0969-2126(98)00049-5
Acta Cryst, pp.8-15, 1998. ,
Development of instrumentation and methods for MAD and structural genomics at the SRS, ESRF, CHESS and Elettra facilities, Journal of Synchrotron Radiation, vol.6, issue.4, pp.822-833, 1999. ,
DOI : 10.1107/S0909049599006172
Anomalous scattering in structural chemistry and biology??, Crystallography Reviews, vol.39, issue.4, pp.245-335, 2005. ,
DOI : 10.1039/cc9960001595
Can anomalous signal of sulfur become a tool for solving protein crystal structures?, Journal of Molecular Biology, vol.289, issue.1, pp.83-92, 1999. ,
DOI : 10.1006/jmbi.1999.2743
Anomalous signal of solvent bromides used for phasing of lysozyme, Journal of Molecular Biology, vol.289, issue.1, pp.93-101, 1999. ,
DOI : 10.1006/jmbi.1999.2744
New approaches to high-throughput phasing, Current Opinion in Structural Biology, vol.12, issue.5, pp.674-678, 2002. ,
DOI : 10.1016/S0959-440X(02)00372-X
Acta Cryst, pp.96-101, 2006. ,
Acta Cryst, pp.2126-2132, 2004. ,
An extensively modified version of MolScript that includes greatly enhanced coloring capabilities, Journal of Molecular Graphics and Modelling, vol.15, issue.2, pp.132-134, 1997. ,
DOI : 10.1016/S1093-3263(97)00021-1
: a program for deriving anomalous-scattering factors from X-ray fluorescence spectra, Journal of Applied Crystallography, vol.34, issue.1, pp.82-86, 2001. ,
DOI : 10.1107/S0021889800014655
Synchrotron Radiation and Biophysics, 1990. ,
macromolecular phasing techniques and associated instrumentation at LURE, Journal of Synchrotron Radiation, vol.6, issue.4, pp.834-844, 1999. ,
DOI : 10.1107/S0909049599006688
High-pressure protein crystallography (HPPX): instrumentation, methodology and results on lysozyme crystals, Journal of Synchrotron Radiation, vol.8, issue.5, pp.1149-1156, 2001. ,
DOI : 10.1107/S0909049501011037
On the treatment of negative intensity observations, Acta Crystallographica Section A, vol.34, issue.4, pp.517-525, 1978. ,
DOI : 10.1107/S0567739478001114
Acta Cryst, pp.315-322, 2003. ,
Acta Cryst, pp.1966-1973, 2003. ,
Macromolecular Crystallography with Synchrotron Radiation, 1992. ,
DOI : 10.1017/cbo9780511524264
Acta Cryst, pp.120-129, 1993. ,
Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur, Nature, vol.206, issue.5802, pp.107-113, 1981. ,
DOI : 10.1038/290107a0
Direct phase determination based on anomalous scattering, Methods Enzymol, vol.115, pp.41-55, 1985. ,
DOI : 10.1016/0076-6879(85)15006-8
Determination of macromolecular structures from anomalous diffraction of synchrotron radiation, Science, vol.254, issue.5028, pp.51-58, 1991. ,
DOI : 10.1126/science.1925561
Maturation of MAD phasing for the determination of macromolecular structures, Journal of Synchrotron Radiation, vol.6, issue.4, pp.845-851, 1999. ,
DOI : 10.1107/S0909049599007591
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, Journal of Applied Crystallography, vol.24, issue.5, pp.946-950, 1991. ,
DOI : 10.1107/S0021889891004399
Solvent content of protein crystals, Journal of Molecular Biology, vol.33, issue.2, pp.491-497, 1968. ,
DOI : 10.1016/0022-2836(68)90205-2
Investigation of possible free-radical scavengers and metrics for radiation damage in protein cryocrystallography, Journal of Synchrotron Radiation, vol.9, issue.6, pp.347-354, 2002. ,
DOI : 10.1107/S0909049502014632
Crank, Structure, vol.12, issue.10, pp.1753-1761, 2004. ,
DOI : 10.1016/j.str.2004.07.018
Physical and chemical considerations of damage induced in protein crystals by synchrotron radiation: a radiation chemical perspective, Journal of Synchrotron Radiation, vol.9, issue.6, pp.329-332, 2002. ,
DOI : 10.1107/S0909049502014553
[20] Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol, vol.276, pp.307-326, 1997. ,
DOI : 10.1016/S0076-6879(97)76066-X
MAD Phasing Strategies Explored with a Brominated Oligonucleotide Crystal at 1.65?? Resolution, Journal of Synchrotron Radiation, vol.3, issue.1, pp.24-34, 1996. ,
DOI : 10.1107/S0909049595013288
Exploring hydrophobic sites in proteins with xenon or krypton, Proteins: Structure, Function, and Genetics, vol.48, issue.1, pp.61-73, 1998. ,
DOI : 10.1002/(SICI)1097-0134(19980101)30:1<61::AID-PROT6>3.0.CO;2-N
Acta Cryst, pp.61-1289, 2005. ,
Phasing in the presence of radiation damage, Journal of Synchrotron Radiation, vol.12, issue.3, pp.276-84, 2005. ,
DOI : 10.1107/S0909049505003286
XOP: Recent developments, SPIE proceedings, vol.3448, 1998. ,
On the preparation and X-ray data collection of isomorphous xenon derivatives, Journal of Applied Crystallography, vol.27, issue.6, pp.950-960, 1994. ,
DOI : 10.1107/S0021889894005923
Protein Crystallography at Ultra-Short Wavelengths: Feasibility Study of Anomalous-Dispersion Experiments at the Xenon K-edge, Journal of Synchrotron Radiation, vol.4, issue.5, pp.287-297, 1997. ,
DOI : 10.1107/S0909049597008571
Acta Cryst, pp.1024-1031, 2004. ,
Structure solution by iterative peaklist optimization and tangent expansion in space group P1, Acta Crystallographica Section B Structural Science, vol.51, issue.4, pp.423-431, 1995. ,
DOI : 10.1107/S0108768195003661
Multi-wavelength anomalous diffraction method for I and Xe atoms using ultra-high-energy X-rays from SPring-8, Journal of Applied Crystallography, vol.37, issue.6, pp.925-933, 2004. ,
DOI : 10.1107/S0021889804023076
Resolution of phase ambiguity in macromolecular crystallography, Methods Enzymol, vol.115, pp.90-112, 1985. ,
DOI : 10.1016/0076-6879(85)15009-3
Sagittal focusing of high-energy synchrotron X-rays with asymmetric Laue crystals. I. Theoretical considerations, Journal of Applied Crystallography, vol.34, issue.4, pp.504-509, 2001. ,
DOI : 10.1107/S0021889801006409
The NIGMS structural biology facility at the NSLS, Synchrotron Radiation News, vol.59, issue.6, pp.20-25, 2003. ,
DOI : 10.1016/S0076-6879(97)76066-X
New approaches to high-throughput phasing, Current Opinion in Structural Biology, vol.12, issue.5, pp.674-678, 2002. ,
DOI : 10.1016/S0959-440X(02)00372-X
Acta Cryst, pp.96-101, 2006. ,
Acta Cryst, pp.2126-2132, 2004. ,
An extensively modified version of MolScript that includes greatly enhanced coloring capabilities, Journal of Molecular Graphics and Modelling, vol.15, issue.2, pp.132-134, 1997. ,
DOI : 10.1016/S1093-3263(97)00021-1
High-pressure protein crystallography (HPPX): instrumentation, methodology and results on lysozyme crystals, Journal of Synchrotron Radiation, vol.8, issue.5, pp.1149-1156, 2001. ,
DOI : 10.1107/S0909049501011037
On the treatment of negative intensity observations, Acta Crystallographica Section A, vol.34, issue.4, pp.517-525, 1978. ,
DOI : 10.1107/S0567739478001114
Acta Cryst, pp.315-322, 2003. ,
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, Journal of Applied Crystallography, vol.24, issue.5, pp.946-950, 1991. ,
DOI : 10.1107/S0021889891004399
Investigation of possible free-radical scavengers and metrics for radiation damage in protein cryocrystallography, Journal of Synchrotron Radiation, vol.9, issue.6, pp.347-354, 2002. ,
DOI : 10.1107/S0909049502014632
Parameters affecting the X-ray dose absorbed by macromolecular crystals, Journal of Synchrotron Radiation, vol.12, issue.3, pp.268-275, 2005. ,
DOI : 10.1107/S0909049505003262
[20] Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol, vol.276, pp.307-326, 1997. ,
DOI : 10.1016/S0076-6879(97)76066-X
Acta Cryst, pp.61-1289, 2005. ,
Unit-cell volume change as a metric of??radiation damage in crystals of macromolecules, Journal of Synchrotron Radiation, vol.9, issue.6, pp.355-360, 2002. ,
DOI : 10.1107/S0909049502014541
Specific Radiation Damage Can Be Used to Solve Macromolecular Crystal Structures, Structure, vol.11, issue.2, pp.217-224, 2003. ,
DOI : 10.1016/S0969-2126(03)00006-6
Structure solution by iterative peaklist optimization and tangent expansion in space group P1, Acta Crystallographica Section B Structural Science, vol.51, issue.4, pp.423-431, 1995. ,
DOI : 10.1107/S0108768195003661
Acta Cryst, pp.1024-1031, 2004. ,
Multi-wavelength anomalous diffraction method for I and Xe atoms using ultra-high-energy X-rays from SPring-8, Journal of Applied Crystallography, vol.37, issue.6, pp.925-933, 2004. ,
DOI : 10.1107/S0021889804023076
On the influence of the incident photon energy on the radiation damage in crystalline biological samples, Journal of Synchrotron Radiation, vol.12, issue.3, pp.304-309, 2005. ,
DOI : 10.1107/S0909049505003328
installation X6A dédiée à la cristallographie des macromolécules. Ma participation est ici presentée aussi sous la forme de deux abstracts. Tous deux sont publiés dans la revue Synchr, pp.20-2523, 2003. ,