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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in complexes with ADP and myo-Ins(1,3,4,5,6)P5, myo-InsP6, neo-InsP6, D-chiro-InsP6, or purpurogallin, sitting drop method, mixing of 5.0-7.5 mg/ml protein solution containing 2 mM ADP and 2 mM ligand with reservoir solution, containing 18 % w/v PEG 3350, 0.1 M bis-Tris propane, pH 6.5, and 2 mM MgCl2, in a 1:1 ratio, and equilibration against 0.05 ml of reservoir solution, 16°C, microseeding X-ray diffraction structure determination and analysis, molecular replacement and modeling
purified recombinant detagged wild-type and mutant enzymes in complex with IP6 and ADP, sitting drop vapor diffusion method, mixing of 20 mg/ml protein solution with crystallization solution containing 0.1 M MES, pH 6.0, 2.1-2.3 M ammonium sulfate, and 10-50 mM TCEP, 22°C, 20% v/v ethylene glycol is used as a cryoprotectant, X-ray diffraction structure determination and analysis at 2.35-2.5 A resolution
purified recombinant detagged enzyme, sitting drop vapour diffusion, mixing of 250 nl of 5-6 mg/ml protein solution with 250 nl of crystallization solution containing 0.2 M MgCl2, 0.1 M MES, pH 6.25, and 18% v/v PEG 6000 for insect cell-expressed enzyme, and 0.2 M MgCl2, 0.1 M MES, pH 6.25, and 12% v/v PEG 6000 for bacteria-expressed enzyme, equilibration against 0.065 ml of crystallization solution as reservoir, method screening and optimization, X-ray diffraction structure determination and analysis at resolution of 4.3 A (Escherichia coli expression) and 4.0 A (insect cell expression), modeling
purified recombinant truncated enzyme lacking the 21 C-terminal residues (DELTAC-mIP5 2-K) in complex with IP5 and ATP or with IP6, X-ray diffraction structure determination and analysis at 2.4-3.2 A resolution. mIP5 2-K cyrstals are not obtained in the absence of inositide, structure for mIP5 2-K in the presence of one or both ligands, forming binary complexes (IP6) or ternary complexes