Crystallization and preliminary crystallographic studies of the butyrolactone autoregulator receptor protein (BarA) from Streptomyces virginiae.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 6): 662-4, 2010 Jun 01.
Article
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| MEDLINE
| ID: mdl-20516594
ABSTRACT
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%.
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Banco de datos:
MEDLINE
Asunto principal:
Fosfotransferasas
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Streptomyces
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Proteínas de la Membrana
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2010
Tipo del documento:
Article
País de afiliación:
Japón