Literature DB >> 25484229

Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei.

Sofiyah Shaibullah1, Nurhikmah Mohd-Sharif1, Kok Lian Ho2, Mohd Firdaus-Raih1, Sheila Nathan3, Rahmah Mohamed4, Chyan Leong Ng1.   

Abstract

Melioidosis is an infectious disease caused by the pathogenic bacterium Burkholderia pseudomallei. Whole-genome sequencing revealed that the B. pseudomallei genome includes 5855 coding DNA sequences (CDSs), of which ∼25% encode hypothetical proteins. A pathogen-associated hypothetical protein, BPSL1038, was overexpressed in Escherichia coli, purified and crystallized using vapour-diffusion methods. A BPSL1038 protein crystal that grew using sodium formate as precipitant diffracted to 1.55 Å resolution. It belonged to space group C2221, with unit-cell parameters a = 85.36, b = 115.63, c = 46.73 Å. The calculated Matthews coefficient (VM) suggests that there are two molecules per asymmetric unit, with a solvent content of 48.8%.

Entities:  

Keywords:  BPSL1038; Burkholderia pseudomallei; hypothetical protein

Mesh:

Substances:

Year:  2014        PMID: 25484229      PMCID: PMC4259243          DOI: 10.1107/S2053230X14025278

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


  21 in total

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