1.2.1.26	dimer	2 * 57000 or 2 * 54351, gel filtration	
1.2.1.26	dimer	2 * 57000 or 2 * 55185, gel filtration	
1.2.1.26	homodimer	2 * 62000, SDS-PAGE	
1.2.1.26	tetramer	gel filtration	
1.2.1.26	tetramer	4 * 52290, calculated from sequence	
1.2.1.26	tetramer	although there are two AbKGSADH molecules in the asymmetric unit of our present structures, the tetrameric structure can be easily generated by one of the two folds from the P4322 crystallographic symmetry operation, structure modeling, overview. The monomeric structure of AbKGSADH consists of three domains: two core domains and one oligomerization domain (OGD). The core domains consist of the N-terminal domain (NTD) (Met1-Arg123 and Val145-Leu253) and the C-terminal domain (CTD) (Gly254-Pro469). The NTD is composed of seven alpha-helices (alpha1-alpha7) and nine beta-strands (beta1-beta4 and beta7-beta11), and forms the NAD(P)-binding Rossmann fold, where seven beta-strands (beta1-beta2 and beta7-beta11) form a large beta-sheet packed in the middle of the domain and other two beta-strands (beta3-beta4) are located on the surface of the domain. The three alpha-helices (alpha1, alpha6 and alpha7) and the four alpha-helices (alpha2-alpha5) occupy both sides of the central beta-sheet. The CTD consists of seven alpha-helices (alpha8-alpha14) and seven beta-strands (beta12-beta18). Seven beta-strands are also packed as a large beta-sheet in the middle of the domain. Six alpha-helices surround the central beta-sheet and one alpha-helix (alpha14) is located between the NTD and the OGD. The OGD (Val124-Pro144 and Tyr470-Val481) has two long beta-strands (beta6 and beta19) and one short beta-strand (beta5), which are packed in a line and protrude from the NTD