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Crystallization and preliminary crystallographic studies of the butyrolactone autoregulator receptor protein (BarA) from<i>Streptomyces virginiae</i>
Description
The Streptomyces butyrolactone autoregulator receptor protein (BarA) is a DNA-binding protein that regulates the biosynthesis of the antibiotic virginiamycin. In this study, BarA from S. virginiae was overexpressed in Escherichia coli, purified and crystallized. Crystals of purified protein have been grown that diffracted to beyond 3.0 A resolution at 100 K using synchrotron radiation. The protein crystals belonged to the hexagonal space group P6(5)22, with unit-cell parameters a = b = 128.0, c = 286.2 A. With four molecules per asymmetric unit, the crystal volume per unit protein mass (V(M)) was 3.2 A(3) Da(-1) and the solvent content was 62%.
Journal
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- Acta Crystallographica Section F Structural Biology and Crystallization Communications
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Acta Crystallographica Section F Structural Biology and Crystallization Communications 66 662-664, 2010-05-26
International Union of Crystallography (IUCr)
