Expression, purification and preliminary X-ray crystallographic analysis of PsaA, a putative metal-transporter protein of Streptococcus pneumoniae

The putative metal‐transporter protein PsaA of Streptococcus pneumoniae is of potential interest both as a vaccine and also as a drug target. The overexpression of the protein in E. coli, and its subsequent purification and crystallization are described. The crystals are rectangular rods and diffrac...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1998-11, Vol.54 (6-2), p.1464-1466
Main Authors: Pilling, Patricia A., Lawrence, Michael C., Berry, Anne M., Ogunniyi, A. David, Lock, Robert A., Paton, James C.
Format: Article
Language:English
Subjects:
Adhesins, Bacterial
Bacterial Proteins
Carrier Proteins - biosynthesis
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - isolation & purification
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Escherichia coli
Lipoproteins - biosynthesis
Lipoproteins - chemistry
Lipoproteins - genetics
Lipoproteins - isolation & purification
Membrane Transport Proteins
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - isolation & purification
Streptococcus pneumoniae - chemistry
Streptococcus pneumoniae - genetics
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Summary:The putative metal‐transporter protein PsaA of Streptococcus pneumoniae is of potential interest both as a vaccine and also as a drug target. The overexpression of the protein in E. coli, and its subsequent purification and crystallization are described. The crystals are rectangular rods and diffract to beyond 2.7 Å resolution. The crystal space group is P212121 with unit‐cell dimensions a = 59.9, b = 66.5 and c = 69.9 Å.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444998005812