901 resultados para isotypic crystal
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Mode of access: Internet.
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"OWR/SPS/99-003."
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"DOWR/SPS/91-001."
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Includes bibliographies.
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Errata pages inserted in vol. 2.
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"AES research and development report"--Cover.
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verso: this is a wreack [sic] we had some time ago, were [sic] you see the cross, the engineer was pined [sic[ two feet in the ground you can imagine what he looked lik [sic]
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The fusion of a protein of interest to a large-affinity tag, such as the maltose-binding protein (MBP), thioredoxin (TRX), or glutathione-S-transferase (GST), can be advantageous in terms of increased expression, enhanced solubility, protection from proteolysis, improved folding, and protein purification via affinity chromatography. Unfortunately, crystal growth is hindered by the conformational heterogeneity induced by the fusion tag, requiring that the tag is removed by a potentially problematic cleavage step. The first three crystal structures of fusion proteins with large-affinity tags have been reported recently. All three structures used a novel strategy to rigidly fuse the protein of interest to MBP via a short three- to five-amino acid spacer. This strategy has the potential to aid structure determination of proteins that present particular experimental challenges and are not conducive to more conventional crystallization strategies (e.g., membrane proteins). Structural genomics initiatives may also benefit from this approach as a way to crystallize problematic proteins of significant interest.