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Acta Crystallogr Sect F Struct Biol Cryst Commun ; 67(Pt 12): 1623-6, 2011 Dec 01.
Article in English | MEDLINE | ID: mdl-22139182

ABSTRACT

Burkholderia pseudomallei BPSL1549, a putative protein of unknown function, has been overexpressed in Escherichia coli, purified and subsequently crystallized by the hanging-drop vapour-diffusion method using PEG as a precipitant to give crystals with overall dimensions of 0.15 × 0.15 × 0.1 mm. Native data were collected to 1.47 Å resolution at the European Synchrotron Radiation Facility (ESRF). The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 37.1, b = 45.4, c = 111.9 Å and with a single polypeptide chain in the asymmetric unit.


Subject(s)
Bacterial Proteins/chemistry , Burkholderia pseudomallei/chemistry , Bacterial Proteins/isolation & purification , Cloning, Molecular , Crystallography, X-Ray
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