期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 164, 期 2, 页码 236-239出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2008.07.007
关键词
Crystallization; MAD phasing; Dissimilatory sulfite reductase; DsrABC complex
资金
- Fundacao para a Ciencia e Tecnologia [PTDC/QUI/68368/06, BIA-PRO/55621/2004]
- FCT-POCTI [SFRH/BD/29519/2006, SFRH/BD/30648/2006]
- ESRF
- SLS [RII3-CT-2004-506008]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/29519/2006, SFRH/BD/30648/2006] Funding Source: FCT
Dissimilatory sulfite reductase (dSiR, DsrAB) is a key protein in dissimilatory sulfur metabolism, one of the earliest types of energy metabolism to be traced on earth. dSirs are large oligomeric proteins around 200 kDa forming an alpha(2)beta(2) arrangement and including a unique siroheme-[4Fe-4S] coupled cofactor. Here, we report the purification, crystallization and preliminary X-ray diffraction analysis of dSir isolated from Desulfovibrio vulgaris Hildenborough, also known as desulfoviridin. In this enzyme the DsrAB protein is associated with DsrC, a protein of unknown function that is believed to play an important role in the sulfite reduction. Crystals belong to the monoclinic space group P2(1) with unit-cell parameters a = 122.7, b = 119.4 and c = 146.7 angstrom and beta =110.0 degrees, and diffract X-rays to 2.8 angstrom on a synchrotron source. (C) 2008 Elsevier Inc. All rights reserved.
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