Cryo bio-crystallography: Difference between revisions
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==Usefulness and applications== |
==Usefulness and applications== |
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Crystallography of large biological macromolecules can be achieved while maintaining their solution state. The best known example is the [[ribosome]].<ref>{{cite journal |author=Hope H |title=Cryocrystallography of biological macromolecules: a generally applicable method|journal=Acta Crystallogr. B|volume=44 |issue=1 |pages=22–26 |year=1988 |pmid=3271102 |doi=10.1107/s0108768187008632}}</ref> |
Crystallography of large biological macromolecules can be achieved while maintaining their solution state. The best known example is the [[ribosome]].<ref>{{cite journal |author=Hope H |title=Cryocrystallography of biological macromolecules: a generally applicable method|journal=Acta Crystallogr. B|volume=44 |issue=1 |pages=22–26 |year=1988 |pmid=3271102 |doi=10.1107/s0108768187008632|bibcode=1988AcCrB..44...22H }}</ref> |
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Today, liquid nitrogen cryo cooling is used for protein crystallography at every synchrotron around the world. Radiation damaged is reduced by more than 70 fold at cryo temperatures. A recent review paper explains the development of reduced radiation damage in macromolecular crystals at Synchrotrons and describes how more than 90% of all structures deposited in the Protein Data Bank used cryo cooling in their determination. |
Today, liquid nitrogen cryo cooling is used for protein crystallography at every synchrotron around the world. Radiation damaged is reduced by more than 70 fold at cryo temperatures. A recent review paper explains the development of reduced radiation damage in macromolecular crystals at Synchrotrons and describes how more than 90% of all structures deposited in the Protein Data Bank used cryo cooling in their determination. |
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1970 Haas, D.J., and Rossmann, M.G. |
1970 Haas, D.J., and Rossmann, M.G. |
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Crystallographic Studies on Lactate Dehydrogenase at -75 C. Acta Crystallogr. (1970), B26, 998. |
Crystallographic Studies on Lactate Dehydrogenase at -75 C. Acta Crystallogr. (1970), B26, 998. |
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*[[X-ray crystallography]] |
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*[[Cryo-EM]] |
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==References== |
==References== |
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{{reflist|1}} |
{{reflist|1}} |
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[[Category:Crystallography]] |
[[Category:Crystallography]] |
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Latest revision as of 05:57, 24 September 2024
Cryo bio-crystallography is the application of crystallography to biological macromolecules at cryogenic temperatures.
Basic principles
[edit]Cryo crystallography enables X-ray data collection at cryogenic temperatures, typically 100 K.
- Crystals are transferred from the solution they have grown in (called mother liquor) to a solution with a cryo-protectant to prevent ice formation.
- Crystals are mounted in a glass fiber (as opposed to a capillary.)
- Crystals are cooled by dipping directly into liquid nitrogen and then placed in a cryo cold stream.
- Cryo cooled macromolecular crystals show reduced radiation damage by more than 70 times that at room temperature.
Advantages
[edit]- Significant improvement of resolution in data collection
- Reduced or eliminated radiation damage in crystals
Usefulness and applications
[edit]Crystallography of large biological macromolecules can be achieved while maintaining their solution state. The best known example is the ribosome.[1] Today, liquid nitrogen cryo cooling is used for protein crystallography at every synchrotron around the world. Radiation damaged is reduced by more than 70 fold at cryo temperatures. A recent review paper explains the development of reduced radiation damage in macromolecular crystals at Synchrotrons and describes how more than 90% of all structures deposited in the Protein Data Bank used cryo cooling in their determination.
2020 Haas, DJ. The early history of cryo-cooling for macromolecular crystallography (2020) IUCrJ (2020). 7, 148–157. https://journals.iucr.org/m/issues/2020/02/00/be5283/be5283.pdf 1970 Haas, D.J., and Rossmann, M.G.
Crystallographic Studies on Lactate Dehydrogenase at -75 C. Acta Crystallogr. (1970), B26, 998.
See also
[edit]References
[edit]- ^ Hope H (1988). "Cryocrystallography of biological macromolecules: a generally applicable method". Acta Crystallogr. B. 44 (1): 22–26. Bibcode:1988AcCrB..44...22H. doi:10.1107/s0108768187008632. PMID 3271102.