Crystallization and preliminary X-ray analysis of wild-type and K272A mutant glutamate 1-semialdehyde aminotransferase from Synechococcus

Journal of Molecular Biology
M HennigJ N Jansonius

Abstract

Crystals of the pyridoxal-5'-phosphate dependent enzyme glutamate-1-semialdehyde aminotransferase (EC 5.4.3.8) 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.

Citations

Jan 11, 2012·Journal of Experimental Botany·Olaf Czarnecki, Bernhard Grimm
May 13, 1997·Proceedings of the National Academy of Sciences of the United States of America·M HennigJ N Jansonius
Jun 1, 1995·Photosynthesis Research·Y J Avissar, P A Moberg
Apr 1, 2007·EcoSal Plus·Samuel I Beale

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