Sun_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_777

Reference

Title : Crystallization and preliminary crystallographic analysis of an esterase with a novel domain from the hyperthermophile Thermotoga maritima - Sun_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_777
Author(s) : Sun L , Levisson M , Hendriks S , Akveld T , Kengen SW , Dijkstra BW , Van der Oost J
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 63 :777 , 2007
Abstract :

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 A resolution. The crystal belongs to space group H32, with unit-cell parameters a = b = 130.2, c = 306.2 A. There are two molecules in the asymmetric unit, with a V(M) of 2.9 A3 Da(-1) and 58% solvent content.

PubMedSearch : Sun_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_777
PubMedID: 17768353
Gene_locus related to this paper: thema-TM0033

Related information

Gene_locus thema-TM0033
Structure thema-TM0033    3DOH    3DOI

Citations formats

Sun L, Levisson M, Hendriks S, Akveld T, Kengen SW, Dijkstra BW, Van der Oost J (2007)
Crystallization and preliminary crystallographic analysis of an esterase with a novel domain from the hyperthermophile Thermotoga maritima
Acta Crystallographica Sect F Struct Biol Cryst Commun 63 :777

Sun L, Levisson M, Hendriks S, Akveld T, Kengen SW, Dijkstra BW, Van der Oost J (2007)
Acta Crystallographica Sect F Struct Biol Cryst Commun 63 :777