期刊
QUARTERLY REVIEWS OF BIOPHYSICS
卷 54, 期 -, 页码 -出版社
CAMBRIDGE UNIV PRESS
DOI: 10.1017/S0033583520000128
关键词
Cryogenic trapping; energy landscape; room temperature; structural dynamics; variable temperature; X-ray crystallography
类别
资金
- ALSAC, St. Jude Children's Research Hospital
This review discusses practical aspects of preparing, acquiring, and analyzing X-ray crystallography data at room temperature, aiming to demystify preconceived impracticalities that freeze progress of routine room temperature data collection at synchrotron sources. Examples are provided as conceptual and experimental templates, illustrating the diversity and utility of gaining novel insights into protein conformational landscapes. An integrative view of protein conformational dynamics offers opportunities to advance basic and biomedical research.
X-ray crystallography enables detailed structural studies of proteins to understand and modulate their function. Conducting crystallographic experiments at cryogenic temperatures has practical benefits but potentially limits the identification of functionally important alternative protein conformations that can be revealed only at room temperature (RT). This review discusses practical aspects of preparing, acquiring, and analyzing X-ray crystallography data at RT to demystify preconceived impracticalities that freeze progress of routine RT data collection at synchrotron sources. Examples are presented as conceptual and experimental templates to enable the design of RT-inspired studies; they illustrate the diversity and utility of gaining novel insights into protein conformational landscapes. An integrative view of protein conformational dynamics enables opportunities to advance basic and biomedical research.
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