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purified recombinant His-tagged native and selenomethionine-labeled enzyme, 12 mg/ml wild-type protein in 25 mM Tris, pH 8.0, and 13.8 mg/ml of selenomethionine-labeled enzyme in 20 mM Tris, pH 8.0, and 5 mM DTT, 4°C, modified microbatch method, equal volumes of protein solution and precipitant solution of 0.001 ml, the latter containing 20%w/v PEG 3350, 0.20 M potassium fluoride, pH 8.5-9.0, are mixed, overlaid with a 1:1 mixture of silicone and paraffin oils, X-ray anomalous diffraction structure determination and analysis at 1.75-2.0 A resolution, molecular replacement
purified wild-type BsIDH and K97V mutant in apo-, holo- and ternary complexes with inositol and inosose, mixing of 0.002 ml of protein solution containing 10mg/ml protein in 25 mM Tris pH 8.0, with 0.002 ml reservoir solution containing 0.1-0.2 M tri-sodium citrate, pH 5.4, and 1.6-2.9 M ammonium sulfate, for the holo-enzyme complexes with 0.1 M tri-sodium citrate pH 5.4, 2.6 M ammonium sulfate and either inositol or inosose at 4 mg/0.1 ml mother liquid, cryoprotection with 25% ethylene glycol, X-ray diffraction structure determination and analysis at 2.3 A resolution
purified recombinant His-tagged enzyme, microbatch crystallization, mixing of 0.001 ml of 10 mg/ml protein in 25 mM Tris-HCl, pH 8.0, with 0.001 ml of crystallization solution containing 2.8 M ammonium sulfate, 0.18 M citric acid, pH 5.0, room temperature, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement and model building, the room-temperature radiation tolerance of a protein crystal and its pseudo-translation symmetry, overview