2.7.1.30	?	? * 56000, SDS-PAGE	641321	
2.7.1.30	?	x * 50000, SDS-PAGE	-, 723070	
2.7.1.30	?	x * 54600, calculated from amino acid sequence	-, 723070	
2.7.1.30	?	x * 56000, deduced from gene sequence	641315	
2.7.1.30	?	x * 56200, calculated from amino acid sequence	-, 723070	
2.7.1.30	?	x * 60400, calculated from amino acid sequence	-, 721188	
2.7.1.30	dimer	2 * 56000, SDS-PAGE, deduced from gene sequence	641319	
2.7.1.30	dimer	crystal structure analysis, probably active state of enzyme	661122	
2.7.1.30	dimer	light scattering analysis confirmed G230D is a dimer and is resistant to tetramer formation in the presence of fructose 1,6-bisphosphate, whereas the wild type enzyme dimers are converted into putatively inactive tetramers in the presence of fructose 1,6-bisphosphate.	678281	
2.7.1.30	dimer	Tk-GK is a dimer in solution in absence of glycerol	-, 761561	
2.7.1.30	dimer or tetramer	2 or 4 * 60000, in solution, the enzyme exists in a dimer-tetramer equilibrium	722712	
2.7.1.30	hexamer	Tk-GK has a hexameric form with a threefold axis in the crystal lattice	-, 761561	
2.7.1.30	homodimer	2 * 60400, calculated from amino acid sequence	738553	
2.7.1.30	homodimer	2 x 57289 (501 residues plus an additional six N-terminal residues from the linker region), mass spectrometry	705779	
2.7.1.30	homodimer	crystal structure	702293	
2.7.1.30	homotetramer	dimer-tetramer equilibrium in solution, tetramer in the crystal	701931	
2.7.1.30	monomer	1 * 53000	641288	
2.7.1.30	additional information	in the absence of glycerol, Tk-GK is a dimer in solution. In the presence of its glycerol substrate, it becomes a hexamer consisting of three symmetrical dimers about the threefold axis. Through glycerol binding, all Tk-GK molecules in the hexamer are in closed form as a result of domain-motion. The closed form of Tk-GK has 10fold higher ATP affinity than the open form of Tk-GK. The hexamer structure stabilizes the closed conformation and enhances ATP binding affinity when the glycerol kinase is bound to glycerol	-, 761561	
2.7.1.30	tetramer	-	641309	
2.7.1.30	tetramer	4 * 50000, SDS-PAGE	641328	
2.7.1.30	tetramer	4 * 55000, SDS-PAGE	641294	
2.7.1.30	tetramer	4 * 55000-57000, equilibrium ultracentrifugation in presence of 6 M guanidine HCl, SDS-PAGE	641287	
2.7.1.30	tetramer	4 * 58000, SDS-PAGE	641309, 641325	
2.7.1.30	tetramer	4 * 60000, SDS-PAGE	641287	
2.7.1.30	tetramer	composed of two dimers, crystal structure analysis	661122	
2.7.1.30	tetramer	crystal structure	641320	
2.7.1.30	tetramer	crystal structure analysis, probably inactive state of enzyme	661122