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Results 1 - 6 of 6
EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.19.3- 95291, 95304, 95316
Display the word mapDisplay the reaction diagram Show all sequences 3.4.19.3crystal structure of wild-type and mutant enzyme C142S/C188S determined at 2.2 and 2.7 A resolution 651784
Display the word mapDisplay the reaction diagram Show all sequences 3.4.19.3crystallized from both ammonium phosphate and ammonium sulfate, structure determined at 1.7 A resolution 653129
Display the word mapDisplay the reaction diagram Show all sequences 3.4.19.3crystallographic analysis of enzyme-inhibitor complex with pyroglutaminal and of the mutant enzyme F142, hanging drop vapour diffusion method 652124
Display the word mapDisplay the reaction diagram Show all sequences 3.4.19.3hanging drop vapor diffusion method at 4°C, 1.6 A resolution 723069
Display the word mapDisplay the reaction diagram Show all sequences 3.4.19.3PCP-0SH polar mutants C142S/C188S/E192D andC142S/C188S/E192Q crystallize at a 6.5% PEG4000, while the apolar mutants C142S/C188S/E192A, C142S/C188S/E192I and C142S/C188S/E192V crystallize at a 5.7-6.0% PEG4000. The protein molecules crystallize in two different space groups. E192Q and E192V form isomorphic monoclinic crystals in the space group P2(1), which agree with those of the wild-type PCP and cysteine-free PCP-0SH (C142S/C188S), while E192A, E192D, and E192I form orthorhombic crystals in the space group P2(1)2(1)2(1). In both crystal systems, four subunit (monomer) molecules are contained in the asymmetric unit. A systematic analysis of individual structures indicates that the mutation does not have any significant effect on the overall structure 667733
Results 1 - 6 of 6