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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.13-
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.13in complex with myo-inositol
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.13mutant Y247S/Y251S in the absence and presence of myo-inositol as well as mutant Y246S/Y247S/Y248S/Y251S, both mutant proteins crystallize as monomers, are very similar to one another, and have no change in the active site region
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.13purified recombinant wild-type enzyme and mutant Y253S complexed with 1,2-dibutyroyl-sn-glycero-3-phosphocholine, hanging drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein, 50 mM myo-inositol and 2.5 mM 1,2-dibutyroyl-sn-glycero-3-phosphocholine, with 0.0015 ml of reservoir solution containing 150 mM ammonium acetate, 100 mM sodium acetate, pH 4.6, with 1 mM Mg(NO3)2 (100 mM for the mutant enzymes), and 16-20% PEG 4000, 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.16-2.3 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.13recombinant PI-PLC
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.13wild-type and D274N mutant PI-PLC
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.13X-ray crystal structure
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