EC Number |
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2.6.1.83 | - |
2.6.1.83 | hanging drop vapour diffusion method at room temperature, 1.95 A resolution. The structure of AtDAP-AT is determined using the multiple-wavelength anomalous dispersion method with a seleno-methionine derivative |
2.6.1.83 | in complex with N-(5'-phosphopyridoxyl)-L-glutamate and N-(5'-phosphopyridoxyl)-LL-diaminopimelate, hanging drop vapor diffusion method, using 45% (w/v) (NH4)2SO4, 0.1 M HEPES pH 7.5, 3% (w/v) PEG400 |
2.6.1.83 | modeling of structure based on the structure of the Arabidopsis thaliana enzyme and comparison between strucutre of Arabidopsis thaliana, from Leptospira interrogans, Verrucomicrobium spinosum and Chlamydomonas reinhardtii enzymes |
2.6.1.83 | PEG 3350 |
2.6.1.83 | PEG 3350, sitting drop method |
2.6.1.83 | purified recombinant enzyme in presence of malic acid, hanging drop vapor diffusion method, mixing of 200 nl of a protein/inhibitor solution containing 39 mg/ml protein in 100 mM HEPES-KOH, 20 mM NaCl, 1 mM DTT, pH 7.6, and 200 mM malic acid, with 200 nl of reservoir solution containing 60% v/v T-mate, pH 7.0, 20°C, 8 weeks, X-ray diffraction structure determination and analysis at 2.25 A resolution, molecular replacement using the crystal structure of Chlamydomonas reinhardtii LL-diaminopimelate aminotransferase (PDB ID 3QGU) as search model, model building |
2.6.1.83 | sitting-drop vapor diffusion methodPEG 6000 |
2.6.1.83 | sitting-drop vapour-diffusion method, PEG 3350 |
2.6.1.83 | to 2.3 A resolution. The large donain (Pro85Ser338) consists of 254 residues and has an alpha-beta-alpha sandwich fold. The large domain includes both the pyridoxal phosphate-binding site and the dimerization site. The small domain is composed of the remaining residues, Gly34Ile84 and Ser339Thr441. The small domain has an alpha/beta architecture, with a beta-sheet surrounded by two outer layers alpha-helices |