Crystallization and preliminary crystallographic studies of the butyrolactone autoregulator receptor protein (BarA) from Streptomyces virginiae.
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%.
Protein Design Laboratory, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama 230-0045, Japan.
Young Ho
YH
Yoon
Fumihiro
F
Kawai
Kanako
K
Sugiyama
Sam Yong
SY
Park
Takuya
T
Nihira
Sun Uk
SU
Choi
Yong Il
YI
Hwang
D003460:Crystallization; D018360:Crystallography, X-Ray; D008565:Membrane Proteins / Q000737:chemistry*; D010770:Phosphotransferases / Q000737:chemistry*; D013302:Streptomyces / Q000201:enzymology*
D008565:Membrane Proteins; D010770:Phosphotransferases