4.1.1.18	?	? * 80000, SDS-PAGE, under native conditions aggregation of up to 10 subunits	37283	
4.1.1.18	?	x * 24000, recombinant His-tagged enzyme, SDS-PAGE	749226	
4.1.1.18	?	x * 54800, recombinant His6-tagged enzyme, SDS-PAGE	748513	
4.1.1.18	?	x * 80000, equilibrium ultracentrifugation in 6 M guanidine-HCl, SDS-PAGE. Association of the dimeric form to the decamer is concomitant with the increase in ionic strength	-, 37289	
4.1.1.18	?	x * 80000, recombinant enzyme	-, 747594	
4.1.1.18	?	x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length	-, 37293	
4.1.1.18	?	x * 85000, SDS-PAGE	-, 727766	
4.1.1.18	decamer	-	748418	
4.1.1.18	decamer	10 * 80000, SDS-PAGE	37299	
4.1.1.18	decamer	10 * 81000, recombinant His-tagged wild-type and mutant T88S, SDS-PAGE	747396	
4.1.1.18	decamer	the protein is an oligomer of five dimers that associate to form a decamer, X-ray crystallography	714832	
4.1.1.18	decamer	x-ray crystallography	690269	
4.1.1.18	dimer	-	748418	
4.1.1.18	dimer	2 * 42000, SDS-PAGE	654982	
4.1.1.18	dimer	2 * 44000, SDS-PAGE	37290	
4.1.1.18	dimer	2 * 76500, SDS-PAGE	-, 728013	
4.1.1.18	heptamer	7 * 79000, SDS-PAGE	-, 37300	
4.1.1.18	hexamer	isozyme TT1465, crystallization data	-, 666850	
4.1.1.18	homodecamer	-	749366	
4.1.1.18	homodecamer	10 * 81000, X-ray crystallography	716768	
4.1.1.18	homodecamer	a pentamer of homodimers, 10 * 82000, recombinant His6-tagged wild-type enzyme, SDS-PAGE	-, 747369	
4.1.1.18	homodimer	2 * 44000, recombinant His-tagged enzyme, SDS-PAGE	749097, 749101	
4.1.1.18	monomer	1 * 95000, SDS-PAGE	37297	
4.1.1.18	additional information	a mixture of dimers (about 158 kDa) and decamers (about 780 kDa) is present for the enzyme at pH 7.5. Decamers are dominant for AsLdc, dependent on the pH: the highest proportion of decamer for AsLdc (78%) is observed at pH 7.5, while it is reduced to 30% and 57% at pH 5.0 and pH 8.5, respectively	748418	
4.1.1.18	additional information	enzyme interacts strongly with regulatory ATPase variant A, RavA, forming a cage-like structure consisting of two enzyme decamers linked by up to five RavA oligomers. Enzyme activity is not affected by binding to RavA, but complex formation results in stimulation of RavA ATPase activity	665713	
4.1.1.18	additional information	SrLDC functions as a dimer and each monomer consists of two distinct domains, a pyridoxal 5'-phosphate-binding-barrel domain and a sheet domain. A shallow substrate-binding hole is formed at the interface between the sheet domains of two monomers	749097	
4.1.1.18	additional information	three-dimensional structure analysis of enzyme CadA, overview	747396	
4.1.1.18	tetramer	isozyme TT1887, crystallization data	-, 666850