|Journal of the American Society for Mass Spectrometry (2010) 21:1795-801|
|New York Structural Genomics Research Consortium|
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A strategy for increasing the efficiency of protein crystallization/structure determination with mass spectrometry has been developed. ...
This approach combines insights from limited proteolysis/mass spectrometry and crystallization via in situ proteolysis. The procedure seeks to identify protease-resistant polypeptide chain segments from purified proteins on the time-scale of crystal formation, and subsequently crystallizing the target protein in the presence of the optimal protease at the right relative concentration. We report our experience with 10 proteins of unknown structure, two of which yielded high-resolution X-ray structures. The advantage of this approach comes from its ability to select only those structure determination candidates that are likely to benefit from application of in situ proteolysis, using conditions most likely to result in formation of a stable proteolytic digestion product suitable for crystallization.
|metabolism chemistry methods |
|Crystallography, X-Ray Proteins Escherichia coli Proteins Crystallization Mass Spectrometry Protein Conformation Peptide Hydrolases Peptide Fragments |
|11 (Last update: 08/11/2018 5:59:28pm)|