1.4.1.13	?	x * 142000 + x * 55000, SDS-PAGE	391454	
1.4.1.13	?	x * 152000 + x * 53000, SDS-PAGE	391462	
1.4.1.13	?	x * 175000 + x * 51500, SDS-PAGE	391460	
1.4.1.13	?	x * 46000, deduced from gene sequence	-, 654888	
1.4.1.13	?	x * 51900, calculated from sequence	745714	
1.4.1.13	?	x * 51900, pGLTY2, SDS-PAGE, x * 52000, pGLTY1, SDS-PAGE	725886	
1.4.1.13	?	x * 52400, calculated from sequence	-, 745714	
1.4.1.13	?	x * 52400, SDS-PAGE	725886	
1.4.1.13	?	x * 72000 + x * 94000	391455	
1.4.1.13	?	x * alpha subunit, 162000, + x * beta subunit, 52300, SDS-PAGE	654382	
1.4.1.13	dimer	1 * 145000 + 1 * 55000, SDS-PAGE	391440	
1.4.1.13	dimer	1 * 158000 + 1 * 54000, SDS-PAGE	391449	
1.4.1.13	dimer	1 * 160000 + 1 * 56000	391459	
1.4.1.13	heterodimer	-	676331	
1.4.1.13	homodimer	2 * 200000, cryoelectron microscopy and small angle X-ray scattering	687801	
1.4.1.13	homohexamer	6 * 200000, cryoelectron microscopy and small angle X-ray scattering, the hexamer exhibits a concentration-dependent equilibrium with monomers and dimers, in solution the hexamer is destabilized by high ionic strength and to a lower extent by the reaction product NADP+	687801	
1.4.1.13	additional information	analysis by synchrotron radiation x-ray solution scattering, alpha subunit and alphabeta holoenzyme are tetrameric in solution, beta subunit is a mixture of monomers and dimers. The (alphabeta)4 holoenzyme is similar to the tetrameric alpha4 complex with the beta subunits occupying the periphery, thus allowing independent catalytic activities of the alphabeta protomers	656149	
1.4.1.13	additional information	modelling of unliganded alpha subunit as well as in complex with L-glutamine and 2-oxoglutarate, subunit exists in a catalytically inactive conformation unable to bind glutamine, and in a catalytically competent conformation, which is stabilized by the glutamine substrate. Binding of L-methionine sulfone causes a coordinated rigid-body motion that results in the inactive conformation	657306	
1.4.1.13	octamer	4 * 135000 + 4 * 50000, SDS-PAGE	391446	
1.4.1.13	octamer	4 * 53000 + 4 * 135000, SDS-PAGE, urea polyacrylamide gel electrophoresis	391438	
1.4.1.13	tetramer	4 * 53000, SDS-PAGE	391464	
1.4.1.13	tetramer	gel filtration, aggregation state of NADPH-GltS alphabeta holoenzyme	676332