scholarly article | Q13442814 |
P356 | DOI | 10.1016/S0969-2126(99)80072-0 |
P698 | PubMed publication ID | 10378275 |
P50 | author | Anne Volbeda | Q54918209 |
P2093 | author name string | E C Hatchikian | |
M Frey | |||
J C Fontecilla-Camps | |||
X Vernede | |||
E Garcin | |||
P2860 | cites work | CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice | Q24286950 |
Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium | Q24561818 | ||
Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus | Q24628999 | ||
PROCHECK: a program to check the stereochemical quality of protein structures | Q26778411 | ||
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures | Q26778412 | ||
Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas | Q27730367 | ||
Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster | Q27734821 | ||
Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis | Q27748809 | ||
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Solvent content of protein crystals | Q27860807 | ||
Refinement of macromolecular structures by the maximum-likelihood method | Q27861011 | ||
The CCP4 suite: programs for protein crystallography | Q27861090 | ||
Comparison of super-secondary structures in proteins | Q28245103 | ||
Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants | Q29546524 | ||
AMoRe: an automated package for molecular replacement | Q29642803 | ||
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Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units | Q34356408 | ||
Carboxy-terminal processing of the large subunit of [NiFe] hydrogenases | Q34357726 | ||
HupUV proteins of Rhodobacter capsulatus can bind H2: evidence from the H-D exchange reaction | Q35618739 | ||
Analysis and comparison of nucleotide sequences encoding the genes for [NiFe] and [NiFeSe] hydrogenases from Desulfovibrio gigas and Desulfovibrio baculatus | Q36177811 | ||
Selenium biochemistry | Q37856267 | ||
Current approaches to macromolecular crystallization | Q37919350 | ||
The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio. | Q39584913 | ||
Hydrogenase | Q40260674 | ||
Nickel hydrogenases: in search of the active site | Q40557814 | ||
Redox properties and activity studies on a nickel-containing hydrogenase isolated from a halophilic sulfate reducer Desulfovibrio salexigens | Q43018686 | ||
Nickel-[iron-sulfur]-selenium-containing hydrogenases from Desulfovibrio baculatus (DSM 1743). Redox centers and catalytic properties. | Q52489982 | ||
Improved Fourier coefficients for maps using phases from partial structures with errors | Q56877556 | ||
X-ray Absorption Spectroscopy of the Molybdenum Site ofEscherichia coliFormate Dehydrogenase | Q57610382 | ||
Biological activition of hydrogen | Q59079237 | ||
Characterization of Representative Enzymes from a Sulfate Reducing Bacterium Implicated in the Corrosion of Steel | Q59287395 | ||
The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743). EPR and Mössbauer characterization | Q68459358 | ||
Effect of 17O2 and 13CO on EPR spectra of nickel in hydrogenase from Chromatium vinosum | Q68491094 | ||
Purification and properties of the soluble hydrogenase from Desulfovibrio desulfuricans (strain Norway 4) | Q72405656 | ||
P433 | issue | 5 | |
P921 | main subject | crystal structure | Q895901 |
P304 | page(s) | 557-566 | |
P577 | publication date | 1999-05-01 | |
P1433 | published in | Structure | Q15709970 |
P1476 | title | The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center | |
P478 | volume | 7 |
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