Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.002 ml of 15 mg/ml protein in 10 mM potassium phosphate, pH 7.0, with 0.002 ml of reservoir solution containing 14.4% PEG 8000, 80 mM cacodylate pH 6.5, 160 mM calcium acetate and 20% glycerol, and equilibration against 0.1 ml of reservoir solution, 25°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.0 A resolution
purified recombinant enzyme in fully closed formation with lactate or pyruvate bound to the active site of each subunit of the functional dimer, 0.001 ml of protein solution containing 20.3 mg/ml protein in 20 mM Tris-HCl buffer pH 8.0 containing 150 mM NaCl, is mixed with 0.001 ml of reservoir solution containing 0.1 M MES buffer, pH 6.0, and 25% w/v PEG 200, 10 days, method optimization, X-ray diffraction structure determination and analysis at 2.12 A resolution, molecular replacement and structure modelling
purified recombinant selenomethionine-labeled enzyme, hanging drop vapour diffusion method, mixing of 0.0015 ml of 35 mg/ml protein in 40 mM Tris-HCl, pH 8.0, and 1 mM DTT with 0.0015 ml of reservoir solution containing 28% w/v PEG 400, 100 mM TrisHCl, pH 9.0, 200 mM magnesium sulfate at 22°C, X-ray diffraction structure determination and analysis at 2.0-2.1 A resolution by single wavelength anomalous dispersion using a selenomethionine derivative