Literature DB >> 22139182

Cloning, purification and crystallographic analysis of a hypothetical protein, BPSL1549, from Burkholderia pseudomallei.

Abimael Cruz-Migoni1, Sergey N Ruzheinikov, Svetlana E Sedelnikova, Barbara Obeng, Sylvia Chieng, Rahmah Mohamed, Sheila Nathan, Patrick J Baker, David W Rice.   

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.

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Year:  2011        PMID: 22139182      PMCID: PMC3232155          DOI: 10.1107/S1744309111028995

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


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