Preliminary crystallographic analysis of 5-carboxymethyl-2-hydroxymuconate isomerase from Escherichia coli.
Escherichia coli 5-carboxymethyl-2-hydroxymuconate (CHM) isomerase was purified from an overexpressing cell line. The enzyme has been crystallized from ammonium sulphate in two different crystal forms. One of these has been analysed and found to be orthorhombic I222 or I2(1)2(1)2(1) with cell dimensions a = 88 A, b = 89 A, c = 121 A. The asymmetric unit contains two dimers (Vm = 2.11 A3/dalton). The crystals diffract to beyond 3.0 A resolution and are stable to irradiation with X-rays. Data have been collected to 3.0 A resolution and a search for potential heavy-metal derivatives is in progress.
Wigley
D B
DB
Department of Biochemistry, University of Leicester, U.K.
Roper
D I
DI
Cooper
R A
RA
D001426:Bacterial Proteins / Q000648:ultrastructure*; D019748:Carbon-Carbon Double Bond Isomerases; D003461:Crystallography; D004926:Escherichia coli / Q000201:enzymology; D007535:Isomerases; D011487:Protein Conformation
D001426:Bacterial Proteins; D007535:Isomerases; D019748:Carbon-Carbon Double Bond Isomerases; C031939:5-carboxymethyl-2-hydroxymuconate delta-isomerase