4.6.1.12	?	x * 17000, SDS-PAGE	657177	
4.6.1.12	?	x * 21348, electrospray mass spectrometry	655417	
4.6.1.12	?	x * 24800, calculated from amino acid sequence	730357	
4.6.1.12	?	x * 25400, calculated from amino acid sequence	730628	
4.6.1.12	?	x * 26100, calculated	681826	
4.6.1.12	?	x * 26100, calculated from sequence	709487	
4.6.1.12	hexamer	complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is observed in solution	656263	
4.6.1.12	additional information	a protein complex assembly of 2-C-methyl-D-erythritol-4-phosphatecytidyltransferase (IspD), CDPME kinase (IspE) and IspF, which catalyze three consecutive steps, is not detectable	-, 747328	
4.6.1.12	additional information	bifunctional 4-diphosphocytidyl-2C-methyl-D-erythritol synthase/2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase enzyme associates in solution with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase, i.e. ispE protein. No evidence for substrate channeling during the three enzyme’s subsequent catalytic reactions	672138	
4.6.1.12	additional information	complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is observed in solution	656263	
4.6.1.12	additional information	the monofunctional enzyme 2C-methyl-D-erythritol-4-phosphate cytidyltransferase and 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase shows physical association	656263	
4.6.1.12	trimer	-	656498, 657196	
4.6.1.12	trimer	3 * 17300	-, 654130	
4.6.1.12	trimer	homotrimeric quarternary structure built around a central hydrophobic cavity and three externally facing active sites	656112