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B6db references: cpamgsa

type Journal Article
authors Hennig, M.; Grimm, B.; Jenny, M.; Muller, R.; Jansonius, J. N.
title Crystallization and preliminary X-ray analysis of wild-type and K272A mutant glutamate 1-semialdehyde aminotransferase from Synechococcus
journal J Mol Biol
ui Cpamgsa
year (1994)
volume 242
number 4
pages 591-4
keywords Crystallization
abstract Crystals of the pyridoxal-5'-phosphate dependent enzyme glutamate-1-semialdehyde aminotransferase (EC from Synechococcus have been grown from polyethylene glycol solutions. The wild-type enzyme crystallizes in space group P2(1)2(1)2(1), with cell dimensions a = 68.4 A, b = 108.0 A, c = 122.6 A. The inactive mutant in which the cofactor-binding lysine 272 residue is replaced by alanine (K272A) gives monoclinic crystals of space group P2(1) with cell dimensions a = 67.1 A, b = 108.6 A, c = 124.5 A and beta = 115.7 degrees. These crystal forms diffract to 2.4 A and 2.7 A resolution, respectively.
last changed 2008/05/21 16:26

B6db references