7.4.2.5	-	699554, 700389	
7.4.2.5	2.8 A resolution crystal structure	669892	
7.4.2.5	crystallization 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	
7.4.2.5	crystals 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	
7.4.2.5	EPR 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	
7.4.2.5	extracellular 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	
7.4.2.5	extracellular 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	
7.4.2.5	homology modeling based on the crystal structure of the Shewanella oneidensis peptide transporter PepTso, identifies Glu56 and Arg305 as potential periplasmic gating residues	719940	
7.4.2.5	molecular 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	
7.4.2.5	recombinant cytosolic ATP-binding domain, N-terminal His-tag	654063