5.4.99.2	-	
5.4.99.2	crystal structure at 2 A resolution of methylmalonyl-CoA mutase in complex with coenzyme B12 and with the partial substrate desulfoCoA	
5.4.99.2	determination of the structure of substrate-free methylmalonyl-CoA mutase is initiated to provide further insight into the mechanism of radical formation	
5.4.99.2	enzyme in the apo, holo, and substrate-bound ternary forms, sitting drop vapor diffusion method, using 1.6 M Na/K-phosphate, 0.1 M HEPES pH 7.5 (apo form), or 30% (w/v) PEG3350, 0.1 M Bis-Tris pH 5.5, 0.3 M (NH4)2SO4 (holo form), or 20% (w/v) PEG3350, 0.1 M Bis-Tris pH 5.5, 0.1 M (NH4)2SO4 (ternary form)	
5.4.99.2	hanging drop method	
5.4.99.2	of the enzymatically inactive inhibitor-protein complex with hydroxycob(III)alamin	
5.4.99.2	vapour diffusion at 23°C	
5.4.99.2	vapour diffusion at 23°C, in the presence of succinyl-CoA, 3-carboxylpropyl-CoA or (2R)-carboxylpropyl-CoA