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Results 1 - 6 of 6
EC Number
hanging drop vapor diffusion method, selenomethionyl enzyme, X-ray structure at 2.5 A of the enzyme with bound UDP
sitting-drop vapor-diffusion method, crystal structures in open and closed conformations. A comparison of these crystal structures shows that upon UDP and UDPGlcNAc binding, the enzyme undergoes conformational changes involving a rigid-body movement of the C-terminal domain
ternary complex between the UDP-GlcNAc 2-epimerase, its substrate UDP-GlcNAc and the reaction intermediate UDP, at 1.7 A resolution. Direct interactions between the substrate and UDP via two hydrogen bonds to the alpha- and beta-phosphates of the adjacent UDP molecule, and between the complex and highly conserved enzyme residues. The binding of UDP-GlcNAc is associated with conformational changes in the active site of the enzyme
UDP-GlcNAc 2-epimerase in complex with UDPGlcNAc and UDP, X-ray diffraction structure determination and analysis at 1.69 A resolution, molecular replacement using enzyme structure, PDB ID 3BEO, as search model
UDP-GlcNAc 2-epimerase in open and closed conformations, and UDP-GlcNAc 2-epimerase in complex with UDPGlcNAc and UDP, sitting drop vapor diffusion method, mixing of 0.001 ml of 5 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 100 mM NaCl, 5% glycerol, and 2 mM tris(2-carboxyethyl)phosphine, with 0.001 ml of reservoir solution containing 40 mM Tris-propane, 60 mM citrate, pH 4.1, and 16% PEG3350, and equilibration against 0.3 ml of reservoir solution at 20°C for 1 week, X-ray diffraction structure determination and analysis at 1.42-2.85 A resolution
vapor diffusion method
Results 1 - 6 of 6