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Results 1 - 10 of 10
EC Number
Crystallization
Reference
2-aminolin-benzoguanine inhibitors in complex with TGT, by hanging-drop, vapor diffusion method at 0°C and macro-seeding, to 1.28-1.78 A resolution, crystals belong to space group C2. The 2-amino-lin-benzoguanines are protonated upon binding to TGT. At pH 5.5, Asp102 is rotated to 75% into the guanine binding pocket whereas at pH 8.5 the same residue is oriented to 100% out of the pocket. Pronounced disorder of the attached side chains addressing the ribose 33 binding pocket
enzyme-inhibitor complexes with 3,5-diaminophthalhydrazide, 4-aminophthalhydrazide, 5-aminonaphthalene-2,3-hydrazide, 5-amino-3-(1H-[1,2,4]triazole-3-yl-sulfanyl)-phthalhydrazide, 5-amino-3-(5-amino-1H-[1,2,4]triazol-3-yl-sulfanyl)-phthalhydrazide. 1.95 A crystal structure of 4-aminophthalhydrazide in complex with the enzyme; in complex with linbenzoguanine (6-aminoimidazol[4,5-g]quinazolin-8(7H)-one), hanging drop vapour diffusion method, in with 100 mM MES buffer (pH 5.5), 1 mM dithiothreitol, 8% (w/v) PEG 8000, 10% DMSO, at 20°C
in complex with 6-amino-4-{2-[(benzylamino)amino]ethyl}-2-[(2-phenylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one trihydrochloride, hanging drop vapor diffusion method
in complex with guanine, pre-queuine 0, and pre-queuine 1, hanging drop vapour diffusion method, in 100 mM MES, pH 5.5, 1 mM dithiothreitol, 13% (w/v) PEG 8000, 10% (v/v) dimethyl sulfoxide
mutant enzyme D280E
mutant K52M, by hanging-drop, vapor-diffusion method and followed by macroseeding, at a resolution of 2.0 A, forms crystals under the same conditions as wild-type, while all attempts to obtain diffracting crystals from mutant Y330F are unsuccessful. Compared to wild-type, crystals of mutant K52M are very fragile and show only a limited diffraction quality
TGT in complex with 6-amino-4-{2-[(cyclohexylmethyl)amino]ethyl}-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one, residues Val45 and Leu68 form a hydrophobic surface that hosts the cyclohexane ring
wild-type and mutant enzyme Y106F, hanging drop method, crystals with a size of approximately 0.7 * 0.7 * 0.2 mm grew within five to seven days
wild-type at pH 5.5 to 1.9 A resolution and in complex with pre-queuine 0 to 1.7 A resolution (both crystals belong to space group C2), and in complex with its natural substrate pre-queuine 1 to 2.4 A resolution (crystal belongs to space group C2221). Mutant Y106F alone to 1.95 A resolution and in complex with pre-queuine 1 to 1.9 A resolution (both crystals belong to space group C2). By macroseeding and the hanging-drop method
Results 1 - 10 of 10