2.7.4.2	1.8 A resolution. Molecule exhibits a compact alpha/beta structure and shows a sulfate molecule tightly bound to the P-loop. This sulfate ion forms hydrogen bonds with the amino group of amino acid G21 and with the side chain of R141	
2.7.4.2	enzyme in a ternary complex with phosphomevalonate, AMPPNP, and Mg2+, by sitting drop method, mixing 0.002 ml of 12 mg/ml PMK in 25 mM HEPES/K+, pH 7.5, 0.25 mM phosphomevalonate, 8 mM AMPPNP, 10 mM MgCl2, with 0.002 ml of 36% w/v PEG 4000, and 100 mM MES/Na+, pH 6.0, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement with EPMR	
2.7.4.2	hanging-drop vapor diffusion at 20°C against a reservoir containing 100 mM HEPES pH 7.5, 800 mM NaH2PO4, 8000 mM KH2PO4 and 30 mM unbuffered ATP, crystals diffract to 2.4 A resolution	
2.7.4.2	NMR-based dynamics and chemical shift experiments of enzyme in complex with MgADP, mevalonate 5-phosphate and the ternary complex. Binding of mevalonate 5-phosphate causes the protein to compress, whereas subsequent binding of MgADP opens the structure. Mevalonate 5-phosphate causes movement around a hinge region to permit domain closure. Amino acids H55 and R93 may act as hinge residues, D163 may be a hinge residue for the lid region. Binding of ATP or ADP causes similar conformational changes. The first nine residues of the N-terminus are highly disordered	
2.7.4.2	purified recombinant His6-tagged enzyme, mixing of 0.002 ml of 10 mg/mL protein in 100 mM (NH4)2SO4, 20 mM HEPES, pH 7.6, with 0.002 ml reservoir solution containing 15% v/v pentaerythritol ethoxylate, 100 mM HEPES, pH 7.6, 15% v/v MPD, 15°C, 2-3 days, X-ray diffraction structure determination and analysis at 1.76 A resolution, SAD method