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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 8(65), p. 853-855, 2009

DOI: 10.1107/s1744309109026670

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Crystallization and preliminary X-ray analysis of the LOV domain of the blue-light receptor YtvA fromBacillus amyloliquefaciensFZB42

Journal article published in 2009 by Hideaki Ogata, Zhen Cao, Aba Losi ORCID, Wolfgang Gärtner
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This paper is available in a repository.

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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%.