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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.2-
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.21.6 A resolution crystal structure
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.2crystal structure determined at 1.5 A resolution by the multiple isomorphous replacement method
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.2crystal structure of PelI is solved to 1.45 A resolution. It consists of an N-terminal domain harboring a fibronectin type III fold linked to a catalytic domain displaying a parallel beta-helix topology. The N-terminal domain is located away from the active site and is not involved in the catalytic process. The structure of PelI in complex with its substrate, a tetragalacturonate, is solved to 2.3 A resolution. The sugar binds from subsites -2 to +2 in one monomer of the asymmetric unit, although it lies on subsites -1 to +3 in the other. These two Michaelis complexes are consistent with the dual mode of bond cleavage in this substrate. The bound sugar adopts a mixed 21 and 31 helical conformation similar to that reported in inactive mutants from families PL-1 and PL-10
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.2crystallization of mutant enzyme C132I/C156N/C194L, hanging-drop vapour-diffusion method
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.2crystallographic analysis of 11 enzyme-Ca2+ complexes formed at pH 4.5, 9.5 and 11.2 under varying Ca2+ concentrations, solved and refined at a resolution of 2.2 A
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.2crystals grown at pH 4.0, to 1.57 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.2hanging drop vapor diffusion method at 18°C, apo form (1.5 A resolution), a metal-bound form of YePL2A (2.0 A resolution) and a trigalacturonic acid-bound substrate complex (2.1 A resolution)
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.2hanging-drop vapor-diffusion method, crystal structure of the PelA T1.5 mutant solved to 1.6 and 2.9 A resolution. Four residues in the T1.5 loop region of PelA are mutated (N215S, T217S, S219G and A220S) to match the structurally analogous T1.5 loop of PelE
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.2hanging-drop vapour-diffusion method at 4°C. The crystals are hexagonal, with unit-cell parameters a = b = 85.55 A, c * 230.13 A, gamma = 120° and belong to space group P6(5)22 or P6(1)22, having one molecule per asymmetric unit
Results 1 - 10 of 25 > >>