ArticleJournal of the American Society for Mass Spectrometry2010
Mass spectrometry guided in situ proteolysis to obtain crystals for X-ray structure determination.
Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Design of an expression system to enhance MBP-mediated crystallization.Scientific reports · 2017Article
- Native mass spectrometry and ion mobility characterize the orange carotenoid protein functional domains.Biochimica et biophysica acta · 2016Article
- Protein stability: a crystallographer's perspective.Acta crystallographica. Section F, Structural biology communications · 2016Review
- Probing the 3-D structure, dynamics, and stability of bacterial collagenase collagen binding domain (apo- versus holo-) by limited proteolysis MALDI-TOF MS.Journal of the American Society for Mass Spectrometry · 2012Article
- Ultra-thin layer MALDI mass spectrometry of membrane proteins in nanodiscs.Analytical and bioanalytical chemistry · 2012Article
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Authors and funding
5 authors.
Funding
Abstract
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.
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