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Results 1 - 10 of 10
EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3database information: http://rebase.neb.com 134254
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3hanging drop vapor diffusion method, using 22% (w/v) polyethylene glycol 8000, 0.02 M imidazole pH 7.5, 5 mM beta-mercaptoethanol 728867
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3hanging-drop and sitting-drop vapour-diffusion method, HsdR subunit crystallized from 8%(w/v) polyethylene glycol 3350, 0.15 M ammonium chloride, 0.1 M HEPES pH 7.5 and 2 mM beta-mercaptoethanol, to 2.60 A resolution. Crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 71.01, b = 89.04, c = 113.66 A. With one HsdR molecule in the asymmetric unit, the Matthews coefficient is 2.14 A3 Da-1 and the solvent content is 42% 695362
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3HsdM subunit, to 1.86 A resolution, by hanging-drop and sitting-drop vapour-diffusion methods. Crystal belongs to the tetragonal space group P41212 or P43212, with unit-cell parameters a = b = 78.9, c = 165.8 A. With one molecule in the asymmetric unit, the crystal volume per unit protein weight is 2.12 A3/Da, with a solvent content of 42% 706964
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3model of subunit HsdR using protein fold-recognition and homology modeling. Subunit shows an ellipsoidal shape of the enzymatic core comprising the N-terminal and central domains. Conformational heterogenity of the C-terminal region implicated in binding of HsdR to the HsdS-HsdM complex 681474
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3motor subunit HsdR of pR124 plasmid-borne type I restriction-modification enzyme EcoR124I, solved in complex with Mg2+-ATP at 2.6 A resolution. HsdR presents four globular domains in a square-planar arrangement, generating prominent grooves between adjacent domain pairs. Lys220 on alpha8 is 3.1 A from N3 on the exposed edge of ATP bound at the helicase domains, potentially coupling endonuclease and helicase function. A uniformly positive surface groove with a clear match to the size and shape of duplex DNA proceeds from a canonical helicase cleft in a continuous path down the front of the motor subunit between the helical and endonuclease domains, where the cleavage site is recessed slightly from the surface 710046
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3N-terminal fragment (ca. 590 amino acids) of a putative HsdR subunit (817 amino acids), native crystals and Se-Met crystals, to 2.5 A resolution, by hanging-drop vapor-diffusion method at 22°C. Se-Met crystal belongs to the orthorhombic space group P212121 with unit-cell dimensions of a = 71.01, b = 89.04 and c = 113.66 A. Seven Se sites in the asymmetric unit at 3.0 A resolution. Crystal structure reveals catalytic sites for nuclease (NTD-domain, Ala21-Ile159) and ATPase (RecA-like domains: RD1 for Lys160-Tyr360 and RD2 for Ala372-Val590) activities and suggests a possible translocation mechanism of the HsdR subunit 710140
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3recombinant motor subunit HsdR of isoform EcoR124I in presence and absence of ATP, at 2.6 A resolution 677379
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3sitting-drop vapor diffusion, crystal structures of three mutants of EcoR124I HsdR are designed to probe this mechanism. The results indicate that interdomain engagement via ATP is responsible for signal transmission between the endonuclease and helicase domains of the motor subunit 751924
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.3sitting-drop vapour-diffusion technique, crystallization and X-ray diffraction data analysis of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I. The shortest of the three encompassed HsdR residues 887-1038 and yielded crystals that belonged to the orthorhombic space group C2221, with unit-cell parameters a = 83.42, b = 176.58, c = 126.03 A, alpha = beta = gamma = 90.0 and two molecules in the asymmetric unit. X-ray diffraction data are collected to a resolution of 2.45 A 749514
Results 1 - 10 of 10