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EC Number
Crystallization
Reference
crystallization of the native and selenomethionyl alanine:glyoxylate aminotransferase is performed using the hanging-drop vapour-diffusion method. Crystal struture is determined at 2.3 A resolution; crystallization of the native and selenomethionyl enzyme is performed using the hanging-drop vapour-diffusion method. Crystal structure is determined at 2.3 A resolution; native enzyme and selenomethionine derivative, to 2.3 A and 2.55 A resolution, respectively. Enzyme is a tetramer. The monomer consists of an N-terminal arm of residues 1–17, a small domain from residues 18–47 and 295–405 and a large domain of residues 48–294. The amino-acid residues involved in cofactor binding are Asn175, Tyr206, Lys234 and Arg242. The guanidino group of Arg361 forms a salt bridge with one carboxylate of the maleate, Thr108 forms a salt bridge with the side-chain carboxylate of the maleate
crystals belong to space group P4(1)2(1)2 or its enantiomorph with uni-cell parameters a = b = 90.81, c = 142.62 A
hanging drop vapour diffusion method with 12% polyethylene glycol 8000, 0.13 M magnesium acetate, 4% butanol, and 0.1 M cacodylic acid at pH 6.5
mutant S187F, to a resolution of 2.9 A. The overall conformation of the variant is similar to that of normal AGTwith a displacement of the PLP-binding Lys209 and Val185, located on the re and si side of PLP, respectively, and slight conformational changes of other active site residues, in particular Trp108, the base stacking residue with the pyridine cofactor moiety. This results in a mispositioning of the AGT-pyridoxamine 5'-phosphate complex and of the external aldimine
using 10% (w/v) PEG 4000 in 0.1 M Na HEPES pH 7.5
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