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EC Number Crystallization (Commentary)
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1-
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1crystal structure at 1.85 A resolution
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1crystal structure at 3 A resolution
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1crystal structure at 6.5 A resolution
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1hanging drop vapor diffusion method, packing of the octameric enzyme in the crystal form is unusual, because the asymmetric unit contains three subunits
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1in complex with Mg2+, hanging drop vapor diffusion method, using 10% (v/v) 2-propanol, 0.1 M MES, pH 6.0, and 0.2 M Ca(OAc)2, or in complex with Mg2+ and cis,cis-muconate, hanging drop vapor diffusion method, using 1.0 M (NH4)2SO4, 0.1 M HEPES, pH 7.0, and 0.5% (w/v) PEG 8000
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1in complex with Mg2+, hanging drop vapor diffusion method, using 20% (v/v) PEG 1000, 0.1 M cacodylate, pH 6.5, and 0.2 M MgCl2, or in complex with Mg2+ and cis,cis-muconate, hanging drop vapor diffusion method, using 2.0 M (NH4)2SO4, 0.1 M MES, pH 6.0, and 5% (v/v) isopropanol
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1muatnt enzyme F329I and I54V
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1sitting-drop vapor diffusion method
Show all pathways known for 5.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.5.1.1the crystallographic structure of the chloromuconate cycloisomerase from Rhodococcus opacus is determined at 2.5 A of resolution. Results highlight that a histidine, located in a loop that closes the active site cavity upon the binding of the substrate, could be related to the dehalogenation inability of Rho-2-CMCI
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