Crystallization and preliminary X-ray diffraction analysis of omega-amino acid:pyruvate transaminase from Chromobacterium violaceum.
The enzyme omega-transaminase catalyses the conversion of chiral omega-amines to ketones. The recombinant enzyme from Chromobacterium violaceum has been purified to homogeneity. The enzyme was crystallized from PEG 4000 using the microbatch method. Data were collected to 1.7 A resolution from a crystal belonging to the triclinic space group P1, with unit-cell parameters a = 58.9, b = 61.9, c = 63.9 A, alpha = 71.9, beta = 87.0, gamma = 74.6 degrees . Data were also collected to 1.95 A from a second triclinic crystal form. The structure has been solved using the molecular-replacement method.
Sayer
Christopher
C
Henry Wellcome Building for Biocatalysis, School of Biosciences, University of Exeter, Exeter EX4 4QD, England.
Isupov
Michail N
MN
Littlechild
Jennifer A
JA
D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism; D002861:Chromobacterium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D019289:Pyruvic Acid / Q000737:chemistry* / Q000378:metabolism; D000637:Transaminases / Q000737:chemistry* / Q000302:isolation & purification
D000596:Amino Acids; D019289:Pyruvic Acid; D000637:Transaminases