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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2007-6-22
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pubmed:abstractText |
The cysteine-rich N-terminal domain of the micronemal adhesive protein MIC1 (MIC1-NT) from Toxoplasma gondii was cloned, expressed in Escherichia coli and purified. MIC1-NT is amenable to structural studies as shown by preliminary NMR and X-ray analysis. Positive results with two further micronemal proteins indicate that our strategy has wider application.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0929-8665
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
411-5
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pubmed:dateRevised |
2009-1-12
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pubmed:meshHeading |
pubmed-meshheading:17584164-Animals,
pubmed-meshheading:17584164-Cell Adhesion Molecules,
pubmed-meshheading:17584164-Chromatography, Gel,
pubmed-meshheading:17584164-Cloning, Molecular,
pubmed-meshheading:17584164-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:17584164-Escherichia coli,
pubmed-meshheading:17584164-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17584164-Protozoan Proteins,
pubmed-meshheading:17584164-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:17584164-Toxoplasma
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pubmed:year |
2007
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pubmed:articleTitle |
High-level bacterial expression and purification of apicomplexan micronemal proteins for structural studies.
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pubmed:affiliation |
Department of Biological Sciences, Division of Molecular Biosciences, Centre for Structural Biology, Imperial College London, South Kensington, London SW7 2AZ, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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