EC Number |
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3.4.19.1 | - |
3.4.19.1 | by hanging drop method. AAP crystallized with the product-like inhibitors Ac-Phe and Gly-Phe, as well as with the substrate Abz-GFEPF(NO2)RA. Mutant S445A crystallized with Abz-GFEPF(NO2)RA. Complexes belong to P212121. Crystal structures of AAPinhibitor complexes reveal the oxyanion-binding site and the specificities of the S1, S2 and S3 subsites. Substrate-binding site extends beyond the S2 subsite, being capable of binding peptides with a longer N-terminus. The S2 subsite displays a non-polar character. The S3 site reveals a hydrophobic region that does not form hydrogen bonds with the inhibitor P3 residue. The enzymeinhibitor complexes reveal that, upon ligand-binding, the S1 subsite undergoes significant conformational changes |
3.4.19.1 | crystallized in mother liquor containing 0.1 M TrisHCl pH 7.0, 10%(w/v) polyethylene glycol 8000, 50 mM MgCl2 and 1%(w/v) CHAPS using the hanging-drop vapour-diffusion technique, 3.4 A resolution, space group C222, unit-cell parameters a = 84.8 A, b = 421.1 A, c = 212.0 A, four molecules in the asymmetric unit |
3.4.19.1 | crystallized using microbatch-under-oil employing the random microseed matrix screening method. The protein crystallizes in space group P2(1)1, with unit-cell parameters a: 77.6, b: 189.6, c: 120.4 A, beta: 108.4 |
3.4.19.1 | crystals are grown at 20°C by the hanging drop method |
3.4.19.1 | crystals grown at 17.8°C using ammonium phosphate as a precipitant. Crystals belong to space group P1 with unit-cell parameters a = 107.5, b = 109.9, alpha = 108.1°, beta = 109.8° and gamma = 91.9° |
3.4.19.1 | crystals of the H367A mutant grown at 20°C in hanging drops, to 2.2 A resolution. Belongs to space group P212121 |
3.4.19.1 | hanging drop method, crystal structure determination of the native and two mutant structures (D524N and D524A) |
3.4.19.1 | hanging-drop vapor diffusion method, 2.5 A resolution, space group: P2(1)2(1)2(1), unit cell parameters: a = 63.1 A, b = 102.3 A, c = 163.9 A, truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is cloned and expressed in Escherichia coli |
3.4.19.1 | hanging-drop vapor-diffusion method. The best crystals were obtained from reservoir of 6% PEG4000, 50 mM/l NaAc (pH 4.6), 15 mM/l DTT, 0.2 mM/l EDTA |