Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of an ASCH domain-containing protein from Zymomonas mobilis ZM4.

ABSTRACT: The human activating signal cointegrator 1 (ASC-1) homology (ASCH) domain is frequently observed in many organisms, although its function has not yet been clearly defined. In Zymomonas mobilis ZM4, the ZMO0922 gene encodes a polypeptide that includes an ASCH domain (zmASCH). To provide a better structural background for the probable role of ASCH domain-containing proteins, the ZMO0922 gene was cloned and expressed. The purified protein was crystallized from 30%(w/v) polyethylene glycol 400, 0.1?M cacodylic acid pH 6.5 and 0.2?M lithium sulfate. Diffraction data were collected to 2.1?Å resolution using synchrotron radiation. The crystal belonged to the primitive trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a=b=51.67, c=207.30?Å, ?=?=90, ?=120°. Assuming the presence of one molecule in the asymmetric unit gave a Matthews coefficient of 4.69?Å(3)?Da(-1), corresponding to a solvent content of 73.7%.

SUBMITTER: Park SY 

PROVIDER: S-EPMC3053153 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature