4.1.1.33	-	
4.1.1.33	hanging drop vapor diffusion method, using 0.25 M sodium formate and 16% (w/v) PEG 3350	
4.1.1.33	hanging drop vapour diffusion method using 0.1 M Tris-HCl (pH 8.0), 1.8 M sodium malonate	
4.1.1.33	in complex wih adenosine 5'-(beta,gamma-imido)-triphosphate and Mg2+	
4.1.1.33	MDD bound to diphosphoglycolyl proline and 6-fluoromevalonate diphosphate, hanging drop vapor diffusion method, using 0.25 M sodium formate and 16% (w/v) PEG 3350, at 20°C	
4.1.1.33	molecular docking of inhibitor eriochrome black A, binds to the active site	
4.1.1.33	molecular docking of inhibitors 6-fluoromevalonate diphosphate and diphosphoglycolylproline	
4.1.1.33	purified enzyme in complex with (R)-5-diphosphomevalonate and adenosine 5'-O-(3-thio)triphosphate or with (R)-5-diphosphomevalonate and ADP, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution	
4.1.1.33	vapour diffusion method, with 0.1 M MES buffer pH 6.5, 20% PEG 5000 MME, 0.1 M NaCl, 1 mM dithiothreitol, and 0.2 M ammonium sulfate	
4.1.1.33	wild-type and mutant S192A and D283A ternary complexes with inbhibitor 6-fluoromevalonate 5-diphosphate and ATPgammaS. During the catalytic mechanism, Asp283 correctly positions the mevalonate diphosphate acceptor substrate, while functioning as a catalytic base to abstract the acidic proton found on its C3-hydroxyl. This deprotonation facilitates an in-line transfer of the gamma-phosphoryl from the ATP donor. The Ser 107 side chain is appropriately positioned to hydrogen bond with both the beta- and gamma-phosphoryl groups of ATPgammaS within the ternary structure