Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis

被引：2
|
作者：
Kurz, M. [1 ,2 ]
Iturbe-Ormaetxe, I. [1 ]
Jarrott, R. [1 ,2 ]
O'Neill, S. L. [1 ]
Byriel, K. A. [1 ,2 ]
Martin, J. L. [1 ,2 ]
Heras, B. [1 ,2 ]
机构：
[1] Univ Queensland, Inst Mol Biosci, Sch Integrat Biol, St Lucia, Qld 4072, Australia
[2] Univ Queensland, ARC Special Res Ctr Funct & Appl Genom, St Lucia, Qld 4072, Australia
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷
关键词：
D O I：
10.1107/S1744309108000055
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
alpha-DsbA1 is one of two DsbA homologues encoded by the Gram-negative alpha-proteobacterium Wolbachia pipientis, an endosymbiont that can behave as a reproductive parasite in insects and as a mutualist in medically important filarial nematodes. The alpha-DsbA1 protein is thought to be important for the folding and secretion of Wolbachia proteins involved in the induction of reproductive distortions. Crystals of native and SeMet alpha-DsbA1 were grown by vapour diffusion and belong to the monoclinic space group C2, with unit-cell parameters a = 71.4, b = 49.5, c = 69.3 angstrom, beta = 107.0 degrees and one molecule in the asymmetric unit (44% solvent content). X-ray data were recorded from native crystals to a resolution of 2.01 angstrom using a copper anode and data from SeMet alpha-DsbA1 crystals were recorded to 2.45 angstrom resolution using a chromium anode.
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收藏
页码：94 / 97
页数：4
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