EC Number   |
|---|
   3.4.14.5 | - |
| 3.4.14.5 | 10 mg/ml purified recombinant soluble enzyme ectodomain, vapour diffusion method, with 20-25% PEG 3350, 0.2 M MgCl2, Tris, pH 8.5, 15% glycerol, flash-frozen crystals for X-ray diffraction structure determination and analysis at 2.1 A resolution, also preparation and study of a mercury derivative |
| 3.4.14.5 | 20 mg/ml purified enzyme, sitting drop vapour diffusion method, room temperature, several days, from 20-22% PEG 2000, 0.1 ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, covering of the drops with perfluoropolyether oil, humidity control during harvest of crystals, multiple wavelength anomalous dispersion using a mercury derivative and subsequent noncrystallographic symmetry averaging, structure determination and analysis, modeling |
| 3.4.14.5 | 20 mg/ml purified soluble extracellular domain apoprotein, glycosidase endo-F treated, in 25 mM Tris, pH 7.5, 100 mM NaCl, 2 mM Tris(2-carboxyethyl)phosphine hydrochloride, i.e. TCEP, 5% glycerol, modified microbatch method, hanging drop vapour diffusion method, from 25% PEG 3350, 200 mM MgCl2, 100 mM HEPES, pH 7.5, complexing with inhibitor 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano(S)-pyrrolidine, several days, X-ray diffraction structure determination and analysis at 1.9 A resolution, in cryoprotectant solution containing 25% PEG 3350, 20% 1,6-hexanediol, at 100 K |
| 3.4.14.5 | 20 mg/ml recombinant soluble enzyme, sitting drop vapour diffusion method, 293 K, from 180 mM Gly-NaOh, pH 9.5, with 180 mM sodium acetate and 18% PEG 4000, crystal grow 2 weeks after seeding, X-ray diffraction structure determination and analysis at 2.6 A resolution |
| 3.4.14.5 | 40 mg/ml extracellular enzyme region complexed with inhibitor valine-pyrrolidine in 20 mM Tris, pH 8.0, ans 25 mM NaCl, sitting drop vapour diffusion method, mixed with equal volume of reservoir solution containing 0.3 M sodium acetate, 17-18% w/v PEG 4000, 0.1 M Tris, pH 8.0, 2-3 days, X-ray diffraction structure determination and analysis at 2.5 A resolution |
| 3.4.14.5 | crystal structure of apo hDPPIV at 1.9 A resolution, crystal structure of hDPPIV-diprotin B (Val-Pro-Leu) complex at 2.1 A resolution |
| 3.4.14.5 | crystal structure of apo hDPPIV at 1.9 A resolution. Crystal structure of hDPPIV-diprotin B complex at 2.1 A resolution |
| 3.4.14.5 | crystal structure of human CD26/dipeptidyl-peptidase IV in complex with bovine adenosine deaminase reveals a highly amphiphilic interface, structure determined at 3.0 A resolution |
| 3.4.14.5 | crystal structure of the free form of DPPIV and of the enzyme in complex with the first 10 residues of the physiological substrate neuropeptide Y (tNPY). The structure of the enzyme/tNPY complex suggests that bioactive peptides utilize the side opening unique to DPPIV to access the active site. Space group of wild-type enzyme and enzyme/tNPY complex is P2(1). The cell dimensions for wild-type enzyme are a = 121.8 A, b = 124,1 A, c = 1445 A, beta = 114.7°. The cell dimensions for the enzyme /tNPY complex are a = b = 122.5 A, c = 145.3 A, beta = 114.9° |
