Abstract
▪ Abstract Atomic resolution structure determinations of proteins by X-ray crystallography are formidable multidisciplinary undertakings, requiring protein construct design, expression and purification, crystallization trials, phase determination, and model building. Modern mass spectrometric methods can greatly facilitate these obligate tasks. Thus, mass spectrometry can be used to verify that the desired protein construct has been correctly expressed, to define compact domains in the target protein, to assess the components contained within the protein crystals, and to screen for successful incorporation of seleno-methionine and other heavy metal reagents used for phasing. In addition, mass spectrometry can be used to address issues of modeling, topology, and side-chain proximity. Here, we demonstrate how rational use of mass spectrometry assists and expedites high resolution X-ray structure determination through each stage of the process of protein crystallography.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 27, 2002, 7:49 a.m.) |
Deposited | 1 year, 7 months ago (Jan. 6, 2024, 12:57 a.m.) |
Indexed | 11 months, 2 weeks ago (Sept. 14, 2024, 7:13 a.m.) |
Issued | 24 years, 2 months ago (June 1, 2001) |
Published | 24 years, 2 months ago (June 1, 2001) |
Published Print | 24 years, 2 months ago (June 1, 2001) |
@article{Cohen_2001, title={Mass Spectrometry as a Tool for Protein Crystallography}, volume={30}, ISSN={1545-4266}, url={http://dx.doi.org/10.1146/annurev.biophys.30.1.67}, DOI={10.1146/annurev.biophys.30.1.67}, number={1}, journal={Annual Review of Biophysics and Biomolecular Structure}, publisher={Annual Reviews}, author={Cohen, Steven L. and Chait, Brian T.}, year={2001}, month=jun, pages={67–85} }