Crystallization and preliminary crystallographic analysis of an esterase with a novel domain from the hyperthermophile Thermotoga maritima

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 angstrom resolution. The crystal belongs to space group H32, with unit-cell parameters a = b = 130.2, c = 306.2 angstrom. There are two molecules in the asymmetric unit, with a VM of 2.9 angstrom(3) Da(-1) and 58% solvent content