Crystallization and preliminary X-ray analysis of wild-type and K272A mutant glutamate 1-semialdehyde aminotransferase from Synechococcus.
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.
Hennig
M
M
Biozentrum, University of Basel, Switzerland.
Grimm
B
B
Jenny
M
M
Müller
R
R
Jansonius
J N
JN
D003460:Crystallization; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000201:enzymology*; D005971:Glutamates; D019751:Intramolecular Transferases; D007535:Isomerases / Q000737:chemistry*
D005971:Glutamates; C057794:glutamate-1-semialdehyde; D007535:Isomerases; D019751:Intramolecular Transferases; C061049:glutamate-1-semialdehyde 2,1-aminomutase