Crystallization of CprB, an autoregulator-receptor protein from Streptomyces coelicolor A3(2).
CprB, an autoregulator-receptor protein from Streptomyces coelicolor A3(2), was crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 6000 as a precipitant. Three crystal forms (I, II and III) were obtained; crystal forms I and II were useful for structure determination. Form I crystals belong to an orthorhombic system with space group P2(1)2(1)2(1) and diffracted to better than 2.4 A. Form II crystals belong to a tetragonal system with space group P4(1(3))2(1)2.
Natsume
Ryo
R
Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. matsume@jbirc.go.jp
Takeshita
Ryo
R
Sugiyama
Masakazu
M
Ohnishi
Yasuo
Y
Senda
Toshiya
T
Horinouchi
Sueharu
S
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D019281:Dimerization; D004926:Escherichia coli / Q000378:metabolism; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012097:Repressor Proteins / Q000737:chemistry* / Q000235:genetics; D013302:Streptomyces / Q000737:chemistry
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins; D012097:Repressor Proteins