Open AccessCloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of hypothetical protein SCO4226 from Streptomyces coelicolor A3(2)
Author(s) -
Wang Shu,
He YongXing,
Bao Rui,
Teng YanBin,
Ye BoPing,
Zhou CongZhao
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910802575x
Subject(s) - streptomyces coelicolor , escherichia coli , recombinant dna , cloning (programming) , crystallization , resolution (logic) , crystallography , microbiology and biotechnology , chemistry , streptomyces , biology , biochemistry , bacteria , genetics , gene , artificial intelligence , organic chemistry , computer science , programming language
A non‐Pfam hypothetical protein SCO4226 of molecular weight 9 kDa from Streptomyces coelicolor A3(2) was overexpressed in Escherichia coli and the purified recombinant protein was crystallized using the sitting‐drop vapour‐diffusion method. An X‐ray diffraction data set was collected to 2.0 Å resolution. The crystal belonged to space group P 2 1 , with unit‐cell parameters a = 29.67, b = 67.00, c = 34.43 Å, α = γ = 90.00, β = 94.26°.