5.4.3.8	?	x * 45043, calculation from nucleotide sequence	3444	
5.4.3.8	?	x * 45932, calculation from nucleotide sequence	3443	
5.4.3.8	?	x * 46000, SDS-PAGE	3428	
5.4.3.8	?	x * 67000, SDS-PAGE	3419	
5.4.3.8	dimer	-	3432, 727125	
5.4.3.8	dimer	2 * 45000, SDS-PAGE	3438	
5.4.3.8	dimer	2 * 45500, SDS-PAGE, native and recombinant GSA-AT	653764	
5.4.3.8	dimer	2 * 46000, SDS-PAGE	3437	
5.4.3.8	dimer	2 * 46172, calculation from nucleotide sequence	3437	
5.4.3.8	dimer	2 * 56000, SDS-PAGE	-, 3440	
5.4.3.8	dimer	enzyme AtGSA1 forms an asymmetric dimer and displays asymmetry in cofactor binding as well as in the gating-loop orientation	746660	
5.4.3.8	dimer	three-dimensional structure analysis of wild-type and mutant enzymes, overview	-, 747005	
5.4.3.8	homodimer	x-ray crystallography	714041	
5.4.3.8	monomer	1 * 43000, SDS-PAGE	3436	
5.4.3.8	additional information	the overall structure of AtGSA1 consists of three sequentially arranged domains: the N-terminal domain (Val1-Asp63, mature protein) comprises one alpha-helix and a three-stranded antiparallel beta-sheet, the pyridoxamine 5'-phosphate/pyridoxal 5'-phosphate-binding domain (Tyr64-Gly328), which is also the catalytic domain, contains a central seven-stranded beta-sheet with one antiparallel and six parallel beta-strands, and the C-terminal domain (Thr329-Ile434) is composed of a three-stranded antiparallel beta-sheet with four helices covering the outer surface. Asymmetry of AtGSA1 in the gating-loop conformation, overview	746660