30GJ image
Deposition Date 2026-04-23
Release Date 2026-08-19
Last Version Date 2026-09-09
Entry Detail
PDB ID:
30GJ
Keywords:
Title:
W-formate dehydrogenase from Nitratidesulfovibrio vulgaris (Desulfovibrio vulgaris) - Ambient temperature, Serial crystallography
Biological Source:
Method Details:
Experimental Method:
Resolution:
1.93 Å
R-Value Free:
0.22
R-Value Work:
0.18
Space Group:
P 21 21 21
Macromolecular Entities
Polymer Type:polypeptide(L)
Molecule:Formate dehydrogenase, alpha
Gene (Uniprot):fdnG-1
Chain IDs:A
Chain Length:1013
Number of Molecules:1
Biological Source:Nitratidesulfovibrio vulgaris str. Hildenborough
Polymer Type:polypeptide(L)
Molecule:Formate dehydrogenase, beta s
Gene (Uniprot):DVU_0588
Chain IDs:B
Chain Length:215
Number of Molecules:1
Biological Source:Nitratidesulfovibrio vulgaris str. Hildenborough
Primary Citation
Room-temperature crystal structure of a metal-dependent W-formate dehydrogenase by serial synchrotron crystallography.
Acta Crystallogr D Struct Biol 82 1072 1081 (2026)
PMID: 42572941 DOI: 10.1107/S2059798326006923

Abstact

Metal-dependent formate dehydrogenases (Fdhs) are a promising research target in efforts to mitigate climate change by developing active, efficient, selective and safe industrial catalysts for CO(2) reduction. Here, we report the room-temperature (RT) serial synchrotron X-ray crystallography (SSX) structure of Nitratidesulfovibrio vulgaris formate dehydrogenase AB and compare this structure with previously reported cryogenic structures. The comparison reveals structural differences likely arising from the absence of cryoprotectants, differences in data-collection temperature and the much lower radiation dose accumulated by each crystal during the SSX experiments. The RT-SSX structure provides the first step towards time-resolved serial crystallography experiments targeting possible catalytic intermediates in order to fully understand the catalytic mechanism of metal-dependent Fdhs.

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