5.4.99.13	additional information	-	size exclusion chromatography yields an estimated molecular mass of 135 kDa, consistent with the large subunit being a homodimer. The recombinant small subunit of PCM is purified as N-terminally His6-tagged protein and elutes with an apparent mass of 20 kDa in gel filtration, suggesting that it exists as a monomer based on the predicted mass of the polypeptide of 17.7 kDa. Gel filtration of a 1:1 mixture of the large and small subunits ofthe enzyme in presence of 5'-deoxyadenosylcobalamin, shows no evidence of complex formation, indicating weak interaction between the subunits under these conditions	748193	
5.4.99.13	14300	-	alpha2beta2, IcmA2IcmB2, 2 * 62500 + 2 * 14300, gel filtration, IcmB provides the cobalamin-binding domain	648802	
5.4.99.13	20000	-	recombinant detagged enzyme, small subunit monomer, gel filtration	748193	
5.4.99.13	62500	-	alpha2beta2, IcmA2IcmB2, 2 * 62500 + 2 * 14300, gel filtration, IcmB provides the cobalamin-binding domain	648802	
5.4.99.13	65000	-	IcmA, 1 * 65000 + several proteins of lower mass, SDS-PAGE	648803	
5.4.99.13	135000	-	recombinant detagged enzyme, large subunit dimer, gel filtration	748193	
5.4.99.13	153000	-	gel filtration	648802