Article ; Online: X-ray free electron lasers motivate bioanalytical characterization of protein nanocrystals: serial femtosecond crystallography.
2013 Volume 85, Issue 7, Page(s) 3464–3471
Abstract: Atomic resolution structures of large biomacromolecular complexes can now be recorded at room temperature from crystals with submicrometer dimensions using intense femtosecond pulses delivered by the world's largest and most powerful X-ray machine, a ... ...
Abstract | Atomic resolution structures of large biomacromolecular complexes can now be recorded at room temperature from crystals with submicrometer dimensions using intense femtosecond pulses delivered by the world's largest and most powerful X-ray machine, a laser called the Linac Coherent Light Source. Abundant opportunities exist for the bioanalytical sciences to help extend this revolutionary advance in structural biology to the ultimate goal of recording molecular-movies of noncrystalline biomacromolecules. This Feature will introduce the concept of serial femtosecond crystallography to the nonexpert, briefly review progress to date, and highlight some potential contributions from the analytical sciences. |
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MeSH term(s) | Animals ; Crystallography, X-Ray/instrumentation ; Crystallography, X-Ray/methods ; Equipment Design ; Humans ; Lasers ; Nanoparticles/chemistry ; Proteins/chemistry |
Chemical Substances | Proteins |
Language | English |
Publishing date | 2013-04-02 |
Publishing country | United States |
Document type | Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Review |
ZDB-ID | 1508-8 |
ISSN | 1520-6882 ; 0003-2700 |
ISSN (online) | 1520-6882 |
ISSN | 0003-2700 |
DOI | 10.1021/ac303716r |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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