EC Number   |
|---|
   3.5.1.93 | - |
| 3.5.1.93 | hanging-drop vapor diffusion method using ammonium sulfate as a precipitating agent, crystal structures of the recombinant selenomethionyl native and S170A mutant precursor |
| 3.5.1.93 | hanging-drop vapour diffusion method, mutant enzymes Y202L, R226K, S170C and E159Q |
| 3.5.1.93 | ligand bound enzyme crystals grow at 21°C from hanging drops, binary complex structure of the enzyme with glutaryl-7-aminocephalosporanic acid and glutarate solved at 2.6 A and 2.5 A resolution, respectively, shows extensive interactions between the glutaryl moiety of glutaryl-7-aminocephalosporanic acid and the seven residues that form the side-chain pocket |
| 3.5.1.93 | polyethylene glycol 6000 as precipitant. The crystals are orthorhombic and have unit-cell parameters a = 141.41, b = 192.0, c = 80.75 A. They belong to a space group P2(1)2(1)2(1) and diffract to at least 2.7 A resolution |
| 3.5.1.93 | preliminary crystals of the double mutant can be grown from 4% PEG 8000, 100 mM Tris-HCl, pH 8.5, carried out by vapour diffusion using hanging-drop method at 17.85°C, 1.57 A resolution |
| 3.5.1.93 | recombinant wild-type enzyme, and unaltered mutant and selenomethionine-labeled mutant H57betaS/H70betaS enzyme, hanging drop vapour diffusion method, reservoir solutions containing 30% PEG, 20% glycerol, and 100 mM Tris, pH 8.0, for 2-4 h, the crystals are cryoprotected using paratone, X-ray diffraction structure determination and analysis at 1.57-2.48 A resolution, modeling |
| 3.5.1.93 | the crystals of Y202L mutants including intermediates, Y202L-I, Y202-II and Y202L-II, and Q168P and L379N are grown at 22°C using the hanging-drop vapor diffusion method. The three dimensional structures are determined at 2-2.5 A resolution. The pro-segments of the mutants undergo dynamic conformational changes during activation and adopt different loop conformations from one another. The autoproteolytic site is found to form catalytically competent conformation with a solvent water molecule, which is essentially conserved in the cephalosporin acylase mutants |
| 3.5.1.93 | vapour diffusion method. Binary complex structures with glutarate and glutaryl-7-aminocephalosporanic acid, solved at 2.6 A and 2.5 A resolution, respectively |
| 3.5.1.93 | vapour-diffusion method. A bipyramidal crystal form is obtained from a solution containing polyethylene glycol and CaCl2. The crystal is tetragonal with the space group P4(1)2(1)2 or P4(3)2(1)2 and the unit cell parameters are a = b = 73.5 A, c = 380.3 A |
