2.7.1.30	-	641286, 641294, 641295, 641299, 641300, 641317, 641327, 702293, 705779	
2.7.1.30	crystals are grown at 20°C by the sitting-drop vapour diffusion method. Native X-ray diffraction data are collected to 2.4 A resolution using synchrotron radiation at station BL44XU of SPring-8. The crystal belongs to the rhombohedral space group R3, with unit-cell parameters a = b = 217.48, c = 66.48 A. The protein is also cocrystallized with substrates and diffraction data are collected to 2.7 A resolution	684168	
2.7.1.30	crystals are obtained by the hanging-drop technique from a solution containing 29% polyethylene glycol 400, 0.1 M sodium acetate pH 4.5, 0.1 M calcium acetate and 10% glycerol. The crystals can grow in the presence of 33% PEG 400, which allows to mount the crystals and directyl flash-cool them. Repeated flash-annealing causes a significant decrease in the averaged mosaicity along with an increase in the overall peak counts of reflections and an enhanced signal-to-noise ratio. Individual reflection-profile analysis reveales a mostly dual domain structure, showing the minimization of one domain as a result of flash-annealing.	677308	
2.7.1.30	crystals of native and mutant enzyme with bound glycerol, hanging drop vapor diffusion method	661122	
2.7.1.30	in complex with glycerol, ADP and the allosteric effector enzyme IIAGlc	661122	
2.7.1.30	in complex with glycerol, in presence and absence of fructose 1,6-diphosphate, mechanism	641326	
2.7.1.30	in complex with substrates, sitting drop vapor diffusion method, using M HEPES pH 7.5, 11% (v/v) hexane-1,6-diol, 25% (w/v) PEG400	739102	
2.7.1.30	of wild type and mutant A65T, both in complex with glycerol and ADP, and of mutant I474D, in complex with IIAGlc	641320	
2.7.1.30	purified recombinant His6-tagged enzyme in complex with pNPP, sitting drop method, mixing of 0.001 ml of 5 mg/mL TbgGK in 10 mM MgSO4, 20 mM NaCl, 0.001% glycerol and 10 mM MOPS, pH 6.8, with 0.001 ml of 11% 1,6-hexanediol, 25% PEG 400, and 0.1 M HEPES, pH 7.5, at 20°C, crystals of the TbgGK-pNPP complex are obtained by soaking TbgGK crystals in a cryoprotectant solution containing 5.5% 1,6-hexanediol, 40% PEG 400, and 0.1 M HEPES, pH 7.5, that is supplemented with 20 mM pNPP, at 20°C, for 6-14 h, X-ray diffraction structure determination and analysis, molecular replacement method using the protein structure of the TbgGK-ADP complex (PDB ID 3WXL) as a search model	760620	
2.7.1.30	purified recombinant wild-type enzyme in complex with glycerol and AMPPCP, and enzyme mutant K271E free or in complex with glycerol, sitting drop vapor diffusion method, 4-5 mg/ml protein in 5 mM Tris-HCl, pH 7.5, with or without 5 mM glycerol, and 5 mM AMPPCP, is mixed with 0.1 M HEPES, pH 8.0, containing 15% w/v PEG 1000 and 200 mM calcium acetate, 20°C, X-ray diffraction structure determination and analysis at 2.3-3.1 A resolution, molecular replacement using the structure of Tk-GK (PDB ID 2ZF5) as template, modelling	761561	
2.7.1.30	sitting drop vapor diffusion method, using 30% (w/v) PEG 400 and 100 mM HEPES pH 7.0, at 20°C	721188	
2.7.1.30	the crystal structure of glycerol kinase mutant G230D is determined to 2.0 A resolution using a microfluidics based crystallization platform	678281	
2.7.1.30	using modified microfluidic scale-up diffraction device, crystals form after one week at ambient temperature unter crystallization conditions 0.3 M magnesium chloride, 0.1 M TrisHCl (pH 8.5), and 20% PEG 1500. Using vapor diffusion crystallization, crystals appear after one week at ambient temperature using the crystallization conditions 0.1 M magnesium chloride, 0.1 M TrisHCl (pH 8.5), and 10% PEG 1500. Glycerol kinase of the mutant G230D crystallied in space group P21 with two tetramers of 222 point symmetry in the asu. The average B factor for the overall structure of the G230D mutant is 21.2 A2.	678281	
2.7.1.30	using sitting-drop vapour-diffusion method at 293 K. Native Tk-glycerol kinase crystals appear after a few days using Wizard I solution No. 25 (0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG 400). Diffraction spots sufficient for structural determination at high resolution are not obtained when a crystal of Tk-glycerol kinase is mounted on a CryoLoop without cryoprotectant, diffraction patterns of the crystal are improved by using Paratone-N as cryoprotectant. Native X-ray diffraction data are collected to 2.4 A resolution using synchrotron radiation at station BL44XU of SPring-8. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = b = 217.48, c = 66.48 A. Assuming the presence of two molecules in the asymmetric unit, the VM value is 2.7 A3Da-1 and the solvent content is 54.1%.	677400