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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of hypothetical protein SCO4226 from Streptomyces coelicolor A3(2).

Authors :
Wang S
He YX
Bao R
Teng YB
Ye BP
Zhou CZ
Source :
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2008 Sep 01; Vol. 64 (Pt 9), pp. 847-50. Date of Electronic Publication: 2008 Aug 20.
Publication Year :
2008

Abstract

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 A resolution. The crystal belonged to space group P2(1), with unit-cell parameters a = 29.67, b = 67.00, c = 34.43 A, alpha = gamma = 90.00, beta = 94.26 degrees .

Details

Language :
English
ISSN :
1744-3091
Volume :
64
Issue :
Pt 9
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology and crystallization communications
Publication Type :
Academic Journal
Accession number :
18765920
Full Text :
https://doi.org/10.1107/S174430910802575X