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Crystallization and preliminary crystallographic analysis of the putative sugar-binding protein Msmeg_0515 (AgaE) from Mycobacterium smegmatis.
Almourfi, Feras M; Rodgers, H Fiona; Sedelnikova, Svetlana E; Baker, Patrick J.
Afiliação
  • Almourfi FM; Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, England.
  • Rodgers HF; Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, England.
  • Sedelnikova SE; Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, England.
  • Baker PJ; Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, England.
Acta Crystallogr F Struct Biol Commun ; 71(Pt 2): 189-93, 2015 Feb.
Article em En | MEDLINE | ID: mdl-25664794
ABSTRACT
Msmeg_0515, a gene from Mycobacterium smegmatis strain 155 encoding the ligand-binding domain, AgaE, of a putative ABC sugar transporter system, has been cloned into a pET-28a vector system, overexpressed in Escherichia coli and purified. The truncated protein lacking the first 27 residues, which correspond to a N-terminal signal sequence, was crystallized using the sitting-drop vapour-diffusion technique. The crystals of this protein diffracted to 1.48 Å resolution and belonged to space group P212121, with unit-cell parameters a = 64.06, b = 69.26, c = 100.74 Å, α = ß = γ = 90° and with one molecule in the asymmetric unit.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Receptores de Superfície Celular / Mycobacterium smegmatis Idioma: En Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Receptores de Superfície Celular / Mycobacterium smegmatis Idioma: En Ano de publicação: 2015 Tipo de documento: Article