title: Crystallization and preliminary diffraction data for adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii.
abstract: Pink crystals of methylmalonyl-CoA mutase from Propionibacterium shermanii, a coenzyme B12 (5'-deoxyadenosylcobalamin)-dependent enzyme, have been obtained by the hanging-drop method in two different forms. One form lies in the space group P21, with unit cell dimensions a = 122 A, b = 160 A and c = 90 A, with beta = 104 degrees (1 A = 0.1 nm). There are two alpha beta dimers in the asymmetric unit. The crystals diffract to 3.2 A resolution and are suitable for high resolution X-ray diffraction studies.
mesh_terms: D003460:Crystallization; D007535:Isomerases; D008765:Methylmalonyl-CoA Mutase; D011424:Propionibacterium / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D007535:Isomerases; D008765:Methylmalonyl-CoA Mutase