Protein perdeuteration for neutron crystallography
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Date
2019-03-28
Authors
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Publisher
The Physical Society of Japan
Abstract
Protein deuteration by recombinant expression in deuterated minimal media offers advantages to several experimental techniques involving neutron scattering. Perdeuteration improves neutron crystallographic studies of proteins. Although not required, protein perdeuteration offers advantages regarding crystal size, data collection time, and the clarity of the resulting experimental nuclear density maps. The level of advantage of perdeuteration depends on practical matters of the existing method of protein production. If recombinant expression yields are high, and purification is efficient, the staff and consumable costs for protein perdeuration are not so great. ©2019 The Physical Society of Japan under the terms of the Creative Commons Attribution 4.0 License
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Keywords
Protein denaturation, Deuteration, Neutrons, Crystallography, Proteins, Yields, Chemical reactions
Citation
Duff, A. P. (2019). Protein perdeuteration for neutron crystallography. Paper presented to the 3rd International Symposium of Quantum Beam Science at Ibaraki University, Japan, May 30 - June 2 2018, "Quantum Beam Science in Biology and Soft Materials (ISQBSS2018). In Journal of the Physical Society of Japan, 25, ISQBSS2018. doi:10.7566/JPSCP.25.011003