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EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.5- 699554, 700389
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.52.8 A resolution crystal structure 669892
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.5crystallization by hanging-drop vapour-diffusion technique in two different space groups P2(1(2))21 (a = b = 168.6 A, c = 149.8 A) and P6(1(5))22 (a = b = 130.9 A, c = 564.6 A). The crystals, improved by macroseeding, diffract to beyond 2.8 A and 3.5 A resolution for the trigonal and hexagonal crystal forms, respectively 667100
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.5crystals diffracting to 2.4 A resolution are obtained using the vapour-diffusion technique with sitting drops. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 203.4, b = 49.8, c = 100.8 A, alpha = gamma = 90.0°, beta = 119°. A selenomethionine derivative is prepared 667081
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.5EPR spectroscopy using covalently attached 2,2,5,5-tetramethylpyrrolidine-1-oxyl spin probes, and 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid spin-labeled peptides. The side-chains' mobility is strongly restricted at the ends of the peptide, whereas the central region is flexible, suggesting a central peptide bulge. Peptides bind to TAP in an extended kinked structure, analogous to those bound to MHC class I proteins 720918
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.5extracellular domain from isoform PepT1, sitting drop vapor diffusion method, using 20% (w/v) polyethylene glycol 6000, 0.1 M MES (pH 6.0), and 0.2 M ammonium chloride 735292
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.5extracellular domain from isoform PepT2, sitting drop vapor diffusion method, using 0.2 M (NH4)3 citrate (pH 5.8) and 21% PEG (w/v) 3350 735292
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.5homology modeling based on the crystal structure of the Shewanella oneidensis peptide transporter PepTso, identifies Glu56 and Arg305 as potential periplasmic gating residues 719940
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.5molecular docking of inhibitor 2-((4-azidobenzyl)thio)-4-(4-(benzyloxy)phenyl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile. The azido group points towards hydrophilic residues including A/Asp512, A/Arg509, A/Gly510 and A/Thr511. The torsion around the -CH2O- atoms between the two phenyl groups allows the terminal phenyl group to rest in a pocket away from the hydrophilic residues B/Thr511, B/Gly510 and B/Glu487. Most of the active inhibitors seem to bind at the interface of chains A and B 733509
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.5recombinant cytosolic ATP-binding domain, N-terminal His-tag 654063
Results 1 - 10 of 12 > >>