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Results 1 - 10 of 14 > >>
EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.132.80 A and 2.04 A resolution crystal structures of inhibitor, beta-thujaplicinol, bound at the RNase H active site of both HIV-1 RT and an isolated RNase H domain. beta-Thujaplicinol chelates two divalent metal ions at the RNase H active site 710577
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.13crystal structure analysis, overview. The pyrimidinol carboxylic acids is successful crystallized with Mn2+ and the isolated HIV RNase H domain 716995
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.13crystal structure of domain swapped Rnase H, overview 751727
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.13determination and analysis of crystal structure of enzyme mutant C280S in complex with inhibitor 6-benzyl-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione, PDB ID 6AOC, hanging drop vapor diffusion method, mixing of 11 mg/ml protein in 10 mM MnCl2, 5 mM tris(2-carboxyethyl)phosphine (TCEP) HCl, 0.5% beta-octylglucoside, and 1 mM 6-benzyl-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione in a 1:1 ratio with crystallization solution containing 15% PEG 3500, 0.1 M sodium potassium phosphate, 5% ethylene glycol, and 0.1 M Tris, pH 6.5, large, blocky crystals grow at 18°C in 2-3 days, molecular replacement using structure PDB ID 4KFB as the initial search model 750467
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.13docking simulation studies. Residue His 539 and two metal ions in the RNase H catalytic center are involved in inhibition by compounds 5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester and 5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester 693579
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.13HIV-1 reverse transcriptase mutant form RT52A in complex with rilpivirine and an RNase H inhibitor XZ462, hanging drop vapor diffusion method, the crystallization solution contains 10% PEG 8000, 50 mM imidazole, pH 6.8, 10 mM spermine, 15 mM MgSO4, and 100 mM (NH4)2SO4, crystals of the RT-rilpivirine (RPV) complex are soaked for 30 min with 2 mM compound XZ462 in the crystallization solution in presence of 15 mM MgSO4, X-ray diffraction structure determination and analysis at 1.51-2.2 A resolution, molecular replacement using the 1.51 A resolution structure of the HIV-1 RT-rilpivirine complex (PDB ID 4G1Q) as template 751430
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.13in complex with substrate, hanging drop vapor diffusion method, using 50 mM Bis-Tris propane-HCl pH 7.0, 10% PEG 8000 (w/v), 100 mM ammonium sulfate, 5% glycerol (v/v), 5% sucrose (w/v) and 20 mM MgCl2 730522
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.13isolated recombinant RNase H domain, to 2.4 A resolution. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of polypeptide p66 is completely inaccessible to solvent in the structure reported here, suggesting that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfolded 701216
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.13modeling of the kinetic refolding intermediate using a C-terminal deletion fragment lacking helix E. Like the kinetic intermediate, this variant folds rapidly and shows a decrease in stability 701113
Display the word mapDisplay the reaction diagram Show all sequences 3.1.26.13purified p66/p51 HIV-1 reverse transcriptase 52A variant in complex with inhibitors manicol and TMC278, 0.0012 ml of 20 mg/mL protein in 9.2 mM Tris, pH 8.0, 68.7 mM NaCl, 3.6 mM manganese sulfate, 0.7 mM tris(2-carboxyethyl) phosphine, 0.27% w/v, beta-ocytl glucopyranoside, 7% v/v DMSO, 0.9 mM manicol, and 0.7 mM TMC278, mixed with 0.0012 ml of reservoir solution containing 50 mM HEPES pH 7.5, 100 mM ammonium sulfate, 15 mM manganese sulfate, 10 mM spermine, 5 mM TCEP, and 11% w/w PEG 8000, X-ray diffraction structure determination and analysis at 2.7 A resolution, modeling 715864
Results 1 - 10 of 14 > >>