Open AccessCrystallization and preliminary crystallographic analysis of an esterase with a novel domain from the hyperthermophile Thermotoga maritima
Author(s) -
Sun Lei,
Levisson Mark,
Hendriks Sjon,
Akveld Twan,
Kengen Servé W. M.,
Dijkstra Bauke W.,
Van Der Oost John
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910703953x
Subject(s) - thermotoga maritima , hyperthermophile , crystallization , crystallography , polyethylene glycol , resolution (logic) , escherichia coli , chemistry , esterase , materials science , biochemistry , archaea , organic chemistry , enzyme , gene , artificial intelligence , computer science
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 H 32, with unit‐cell parameters a = b = 130.2, c = 306.2 Å. There are two molecules in the asymmetric unit, with a V M of 2.9 Å 3 Da −1 and 58% solvent content.