Macromolecular cryocrystallography – methods for cooling and mounting protein crystals at cryogenic temperatures. Pflugrath, J. W. Methods, 34(3):415-423, 2004. Macromolecular Crystallization
Macromolecular cryocrystallography – methods for cooling and mounting protein crystals at cryogenic temperatures [link]Paper  doi  abstract   bibtex   
Cryocrystallography is routinely used in macromolecular crystallography laboratories. The main advantage of X-ray diffraction data collection near 100K is that crystals display much less radiation damage than seen at room temperature. Techniques and tools are described to facilitate cryoprotecting and flash-cooling crystals for data collection.
@article{Pflugrath_2004,
title = {Macromolecular cryocrystallography -- methods for cooling and mounting protein crystals at cryogenic temperatures},
journal = {Methods},
volume = {34},
number = {3},
pages = {415-423},
year = {2004},
note = {Macromolecular Crystallization},
issn = {1046-2023},
doi = {10.1016/j.ymeth.2004.03.032},
url = {https://www.sciencedirect.com/science/article/pii/S1046202304001227},
author = {Pflugrath, J. W.},
keywords = {Cryocrystallography, Cryoprotectants, Flash-cooling, Crystal mounting, Annealing},
abstract = {Cryocrystallography is routinely used in macromolecular crystallography laboratories. The main advantage of X-ray diffraction data collection near 100K is that crystals display much less radiation damage than seen at room temperature. Techniques and tools are described to facilitate cryoprotecting and flash-cooling crystals for data collection.}
}

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