Open AccessCloning, purification, crystallization and preliminary X‐ray crystallographic analysis of MCAT from Synechocystis sp. PCC 6803
Author(s) -
Liu Yinghui,
Zhang Yanming,
Cao Xupeng,
Xue Song
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113026274
Subject(s) - orthorhombic crystal system , crystallization , crystallography , crystal (programming language) , chemistry , crystal structure , enzyme , molecule , resolution (logic) , solvent , biochemistry , organic chemistry , computer science , programming language , artificial intelligence
Malonyl‐coenzymeA:acyl‐carrier protein transacylase (MCAT), which catalyzes the transfer of the malonyl group from malonyl‐CoA to acyl‐carrier protein (ACP), is an essential enzyme in type II fatty‐acid synthesis. The enzyme MCAT from Synechocystis sp. PCC 6803 (spMCAT), the first MCAT counterpart from a cyanobacterium, was cloned, purified and crystallized in order to determine its three‐dimensional crystal structure. A higher‐quality crystal with better diffraction was obtained by crystallization optimization. The crystal diffracted to 1.8 Å resolution and belonged to the orthorhombic space group P 2 1 2 1 2, with unit‐cell parameters a = 43.22, b = 149.21, c = 40.59 Å. Matthews coefficient calculations indicated that the crystal contained one spMCAT molecule in the asymmetric unit with a Matthews coefficient of 2.18 Å 3 Da −1 and a solvent content of 43.65%.