Crystallization and preliminary X-ray analysis of the LOV domain of the blue-light receptor YtvA from Bacillus amyloliquefaciens FZB42.
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%.
Ogata
Hideaki
H
Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
Cao
Zhen
Z
Losi
Aba
A
Gärtner
Wolfgang
W
D001407:Bacillus / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry*; D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D004269:DNA, Bacterial; D004591:Electrophoresis, Polyacrylamide Gel; D008027:Light; D011487:Protein Conformation; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D001426:Bacterial Proteins; D017931:DNA Primers; D004269:DNA, Bacterial