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Title: Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum

Abstract

This article describes the first successful crystallization of a membrane-bound [NiFe] hydrogenase isolated from a photosynthetic organism (A. vinosum). The crystals obtained produced diffraction patterns up to 2.5 Å resolution. The membrane-bound [NiFe] hydrogenase is a unique metalloprotein that is able to catalyze the reversible oxidation of hydrogen to protons and electrons during a complex reaction cycle. The [NiFe] hydrogenase was isolated from the photosynthetic purple sulfur bacterium Allochromatium vinosum and its crystallization and preliminary X-ray analysis are reported. It was crystallized by the hanging-drop vapour-diffusion method using sodium citrate and imidazole as crystallization agents. The crystals belong to space group P2{sub 1}2{sub 1}2, with unit-cell parameters a = 205.00, b = 217.42, c = 120.44 Å. X-ray diffraction data have been collected to 2.5 Å resolution.

Authors:
; ;  [1]
  1. Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr (Germany)
Publication Date:
OSTI Identifier:
22360611
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 64; Journal Issue: Pt 8; Other Information: PMCID: PMC2494966; PMID: 18678940; PUBLISHER-ID: fw5181; OAI: oai:pubmedcentral.nih.gov:2494966; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CITRATES; CRYSTALLIZATION; CRYSTALS; DIFFUSION; ELECTRONS; HYDROGEN; MEMBRANES; OXIDATION; PROTONS; RESOLUTION; SODIUM COMPOUNDS; SPACE GROUPS; SULFUR; X-RAY DIFFRACTION

Citation Formats

Kellers, Petra, Ogata, Hideaki, and Lubitz, Wolfgang. Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum. United Kingdom: N. p., 2008. Web. doi:10.1107/S1744309108019945.
Kellers, Petra, Ogata, Hideaki, & Lubitz, Wolfgang. Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum. United Kingdom. https://doi.org/10.1107/S1744309108019945
Kellers, Petra, Ogata, Hideaki, and Lubitz, Wolfgang. Fri . "Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum". United Kingdom. https://doi.org/10.1107/S1744309108019945.
@article{osti_22360611,
title = {Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum},
author = {Kellers, Petra and Ogata, Hideaki and Lubitz, Wolfgang},
abstractNote = {This article describes the first successful crystallization of a membrane-bound [NiFe] hydrogenase isolated from a photosynthetic organism (A. vinosum). The crystals obtained produced diffraction patterns up to 2.5 Å resolution. The membrane-bound [NiFe] hydrogenase is a unique metalloprotein that is able to catalyze the reversible oxidation of hydrogen to protons and electrons during a complex reaction cycle. The [NiFe] hydrogenase was isolated from the photosynthetic purple sulfur bacterium Allochromatium vinosum and its crystallization and preliminary X-ray analysis are reported. It was crystallized by the hanging-drop vapour-diffusion method using sodium citrate and imidazole as crystallization agents. The crystals belong to space group P2{sub 1}2{sub 1}2, with unit-cell parameters a = 205.00, b = 217.42, c = 120.44 Å. X-ray diffraction data have been collected to 2.5 Å resolution.},
doi = {10.1107/S1744309108019945},
url = {https://www.osti.gov/biblio/22360611}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 8,
volume = 64,
place = {United Kingdom},
year = {2008},
month = {8}
}