Open AccessCrystallization and preliminary crystallographic studies of the butyrolactone autoregulator receptor protein (BarA) from Streptomyces virginiae
Author(s) -
Yoon YoungHo,
Kawai Fumihiro,
Sugiyama Kanako,
Park SamYong,
Nihira Takuya,
Choi SunUk,
Hwang YongIl
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110009930
Subject(s) - virginiamycin , crystallization , crystallography , escherichia coli , resolution (logic) , streptomyces , solvent , chemistry , space group , stereochemistry , biology , bacteria , biochemistry , x ray crystallography , antibiotics , diffraction , gene , organic chemistry , physics , artificial intelligence , computer science , optics , genetics
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 Å resolution at 100 K using synchrotron radiation. The protein crystals belonged to the hexagonal space group P 6 5 22, with unit‐cell parameters a = b = 128.0, c = 286.2 Å. With four molecules per asymmetric unit, the crystal volume per unit protein mass ( V M ) was 3.2 Å 3 Da −1 and the solvent content was 62%.