Improvement of the Diffraction Properties of Thiocyanate Dehydrogenase Crystals
- Autores: Varfolomeeva L.1, Polyakov K.2, Komolov A.3, Rakitina T.3,4, Dergousova N.1, Dorovatovskii P.3, Boyko K.5, Tikhonova T.1, Popov V.1
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Afiliações:
- Federal Research Center “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia
- Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia
- National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia
- Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997, Moscow, Russia
- Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences, 117071, Moscow, Russia
- Edição: Volume 68, Nº 6 (2023)
- Páginas: 888-893
- Seção: STRUCTURE OF MACROMOLECULAR COMPOUNDS
- URL: https://journals.rcsi.science/0023-4761/article/view/231817
- DOI: https://doi.org/10.31857/S0023476123600799
- EDN: https://elibrary.ru/ABAVXD
- ID: 231817
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Resumo
During determination of the thiocyanate dehydrogenase (TcDH) structure difficulties have occurred, related to the fact that enzyme crystals have been either twinned or strongly anisotropic. The diffraction quality of crystals can be improved by using mutant forms as objects of a study or by studying the structure of a related enzyme from another organism. Based on the analysis of the oligomeric structure of TcDH, the mutant forms of the enzyme that are promising for improving the diffraction properties have been proposed. The crystals have been obtained and the structures of the TcDH mutant forms with the substitutions T169A and K281A have been solved. The structure of the mutant form with the substitution T169A is found to be similar to the previously solved structures. In the structure of the mutant form with the substitution K281A, a change in the tetramer structure that made twinning impossible has been detected.
Sobre autores
L. Varfolomeeva
Federal Research Center “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia
Email: larisaavarfolomeeva@gmail.com
Россия, Москва
K. Polyakov
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia
Email: kmpolyakov@gmail.com
Россия, Москва
A. Komolov
National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia
Email: larisaavarfolomeeva@gmail.com
Россия, Москва
T. Rakitina
National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia; Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997, Moscow, Russia
Email: larisaavarfolomeeva@gmail.com
Россия, Москва; Россия, Москва
N. Dergousova
Federal Research Center “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia
Email: larisaavarfolomeeva@gmail.com
Россия, Москва
P. Dorovatovskii
National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia
Email: larisaavarfolomeeva@gmail.com
Россия, Москва
K. Boyko
Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences, 117071, Moscow, Russia
Email: boiko_konstantin@inbi.ras.ru
Россия, Москва
T. Tikhonova
Federal Research Center “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia
Email: larisaavarfolomeeva@gmail.com
Россия, Москва
V. Popov
Federal Research Center “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia
Autor responsável pela correspondência
Email: larisaavarfolomeeva@gmail.com
Россия, Москва
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