| Autor: |
Lei Sun, Levisson, Mark, Hendriks, Sjon, Akveld, Twan, Kengen, Servé W. M., Dijkstra, Bauke W., van der Oost, John |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section F (Wiley-Blackwell); Sep2007, Vol. 63 Issue 9, p777-779, 3p, 1 Color Photograph, 1 Chart |
| Abstrakt: |
A predicted esterase (EstA) with an unusual new domain from the hyperthermophilic bacterium Thermotoga maritima has been cloned and overexpressed in Escherichia coli. The purified protein was crystallized by the hanging-drop vapour-diffusion technique in the presence of lithium sulfate and polyethylene glycol 8000. Selenomethionine-substituted EstA crystals were obtained under the same conditions and three different-wavelength data sets were collected to 2.6 Å resolution. The crystal belongs to space group H32, with unit-cell parameters a = b = 130.2, c = 306.2 Å. There are two molecules in the asymmetric unit, with a VM of 2.9 Å3 Da−1 and 58% solvent content. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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