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Crystallization and preliminary X-ray analysis of the LOV domain of the blue-light receptor YtvA from Bacillus amyloliquefaciens FZB42.

ABSTRACT: Light-oxygen-voltage (LOV) proteins play an important role in blue-light-dependent physiological processes in many organisms. The LOV domain of the blue-light receptor YtvA from Bacillus amyloliquefaciens FZB42 has been purified and crystallized at 277 K using the sitting-drop vapour-diffusion method with 2-ethoxyethanol as a precipitant. A data set was collected to 1.60 A resolution from a single crystal at 100 K using synchrotron radiation. The LOV domain of YtvA crystallized in space group C222(1), with unit-cell parameters a = 64.95, b = 83.76, c = 55.81 A. The crystal structure of the LOV domain of YtvA was determined by the molecular-replacement method. The crystal contained one molecule per asymmetric unit, with a Matthews coefficient (V(M)) of 3.04 A(3) Da(-1); the solvent content was estimated to be 59.5%.

SUBMITTER: Ogata H

PROVIDER: S-EPMC2720352 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of the LOV domain of the blue-light receptor YtvA from Bacillus amyloliquefaciens FZB42.

Ogata Hideaki H Cao Zhen Z Losi Aba A Gärtner Wolfgang W

Acta crystallographica. Section F, Structural biology and crystallization communications 20090730 Pt 8

Light-oxygen-voltage (LOV) proteins play an important role in blue-light-dependent physiological processes in many organisms. The LOV domain of the blue-light receptor YtvA from Bacillus amyloliquefaciens FZB42 has been purified and crystallized at 277 K using the sitting-drop vapour-diffusion method with 2-ethoxyethanol as a precipitant. A data set was collected to 1.60 A resolution from a single crystal at 100 K using synchrotron radiation. The LOV domain of YtvA crystallized in space group C2 ...[more]

PMID: 19652358

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