The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes.
作者信息
Jackson Colin J, Carr Paul D, Kim Hye Kyung, Liu Jian Wei, Ollis David L
机构信息
The Research School of Chemistry, Australian National University, ACT 0200, Australia.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt 7):659-61. doi: 10.1107/S1744309106020021. Epub 2006 Jun 10.
Abstract
The metallo-glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) has been cloned, expressed in Escherichia coli and purified. Initial screening of crystallization conditions for this enzyme resulted in the identification of needles from one condition in a sodium malonate grid screen. Removal of the metals from the enzyme and subsequent optimization of these conditions led to crystals that diffracted to 2.9 angstroms and belonged to space group P2(1)3, with unit-cell parameter a = 164.1 angstroms. Self-rotation function analysis and V(M) calculations indicated that the asymmetric unit contains two copies of the monomeric enzyme, corresponding to a solvent content of 79%. It is intended to determine the structure of this protein utilizing SAD phasing from transition metals or molecular replacement.
摘要
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