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A Periplasmic Glutamate/Aspartate Binding Protein from Shigella flexneri: Gene Cloning, Over-Expression, Purification and Preliminary Crystallographic Studies of the Recombinant Protein

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Periplasmic substrate binding proteins (PSBPs) are essential components of the bacterial periplasmic transport system, which transports a wide variety of nutrients from the periplasmic space to the cytoplasm. The glutamate/aspartate binding protein SfGlu/AspBP is a unique PSBP consisting of 279 amino acid residues. The SfGlu/AspBP gene was cloned, over-expressed, and purified by immobilized metal ion affinity chromatography and size-exclusion chromatography. The recombinant protein SfGlu/AspBP has been crystallized by the hanging-drop vapor-diffusion method and its Xray diffraction data were collected at an atomic resolution of 1.15 Å. The crystals belong to the space group P21 with unit cell parameters: a=48.41 Å, b=68.18 Å, c=80.21 Å and b = 98.78 . There are two molecules per asymmetric unit.

Keywords: Periplasmic glutamate/aspartate binding protein; Shigella flexneri; crystal data; crystallization

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606776819646

Affiliations: Center for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101, People's Republic of China.

Publication date: May 1, 2006

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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