EC Number |
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2.3.2.20 | hanging drop vapor diffusion method, using 10% (w/v) PEG8000, 50 mM KCl, 50 mM sodium cacodylate, pH 6.0 |
2.3.2.20 | purified recombinant enzyme, crystallization from 11% PEG 3350, 0.1 M HEPES, pH 7.5, and 0.2 M L-Pro, X-ray difffraction structure determination and analysis at 3.06 A resolution |
2.3.2.20 | purified recombinant enzyme, crystallization from 15.2% PEG 3350, 0.1 M potassium fluoride, X-ray difffraction structure determination and analysis at 1.99 A resolution |
2.3.2.20 | purified recombinant enzyme, crystallization from 22% PEG 3350, 0.2 M tri-ammonium citrate, pH 7.0, X-ray difffraction structure determination and analysis at 3.18 A resolution |
2.3.2.20 | to 1.9 A resolution, monomer that presents a compact alpha/beta structure. It is composed of a central beta-sheet with five parallel beta strands surrounded by ten alpha helices. AlbC contains a deep pocket, highly conserved among cyclodipeptide synthases. This pocket accommodates the aminoacyl moiety of the aa-tRNA substrate |