Advances in experimental and computational techniques have reaffirmed the role of protein X-ray crystallography as one of the primary providers of structural information both to enhance our fundamental understanding of biological systems and also to assist the design and optimization of important th
Temperature-dependent macromolecular X-ray crystallography
โ Scribed by Weik, Martin ;Colletier, Jacques-Philippe
- Publisher
- International Union of Crystallography
- Year
- 2010
- Tongue
- English
- Weight
- 541 KB
- Volume
- 66
- Category
- Article
- ISSN
- 0907-4449
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โฆ Synopsis
X-ray crystallography provides structural details of biological macromolecules. Whereas routine data are collected close to 100โ K in order to mitigate radiation damage, more exotic temperature-controlled experiments in a broader temperature range from 15โ K to room temperature can provide both dynamical and structural insights. Here, the dynamical behaviour of crystalline macromolecules and their surrounding solvent as a function of cryo-temperature is reviewed. Experimental strategies of kinetic crystallography are discussed that have allowed the generation and trapping of macromolecular intermediate states by combining reaction initiation in the crystalline state with appropriate temperature profiles. A particular focus is on recruiting X-ray-induced changes for reaction initiation, thus unveiling useful aspects of radiation damage, which otherwise has to be minimized in macromolecular crystallography.
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