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Preparation and Crystallization of Picornain 3C of Rhinovirus A28. / Tishin, A. E.; Gladysheva, A. A.; Pyatavina, L. A. и др.

в: Crystallography Reports, Том 68, № 6, 12.2023, стр. 924-930.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Tishin, AE, Gladysheva, AA, Pyatavina, LA, Olkin, SE, Gladysheva, AA, Imatdionov, IR, Vlaskina, AV, Nikolaeva, AY, Samygina, VR & Agafonov, AP 2023, 'Preparation and Crystallization of Picornain 3C of Rhinovirus A28', Crystallography Reports, Том. 68, № 6, стр. 924-930. https://doi.org/10.1134/S1063774523601119

APA

Tishin, A. E., Gladysheva, A. A., Pyatavina, L. A., Olkin, S. E., Gladysheva, A. A., Imatdionov, I. R., Vlaskina, A. V., Nikolaeva, A. Y., Samygina, V. R., & Agafonov, A. P. (2023). Preparation and Crystallization of Picornain 3C of Rhinovirus A28. Crystallography Reports, 68(6), 924-930. https://doi.org/10.1134/S1063774523601119

Vancouver

Tishin AE, Gladysheva AA, Pyatavina LA, Olkin SE, Gladysheva AA, Imatdionov IR и др. Preparation and Crystallization of Picornain 3C of Rhinovirus A28. Crystallography Reports. 2023 дек.;68(6):924-930. doi: 10.1134/S1063774523601119

Author

Tishin, A. E. ; Gladysheva, A. A. ; Pyatavina, L. A. и др. / Preparation and Crystallization of Picornain 3C of Rhinovirus A28. в: Crystallography Reports. 2023 ; Том 68, № 6. стр. 924-930.

BibTeX

@article{82bacf22dbfe4ff1a405fc3a8c72062d,
title = "Preparation and Crystallization of Picornain 3C of Rhinovirus A28",
abstract = "Human rhinovirus picornain 3C is a high-value commercial cysteine protease, which is widely used to remove affinity tags and fusion proteins during the purification of the target proteins. A variant of rhinovirus A28 picornain 3C produced in this study is not annotated in the NCBI databases, shares 79% sequence identity in the PDB, and was not previously used in the protein engineering. A protocol was developed for the isolation and purification of the protein to use it in structural studies. The initial crystallization conditions were found. The determination and analysis of the structure of rhinovirus A28 picornain 3C will provide new possibilities for performing basic research on the evolution of proteolytic enzymes and for the design of the optimal variant of this protease.",
author = "Tishin, {A. E.} and Gladysheva, {A. A.} and Pyatavina, {L. A.} and Olkin, {S. E.} and Gladysheva, {A. A.} and Imatdionov, {I. R.} and Vlaskina, {A. V.} and Nikolaeva, {A. Yu} and Samygina, {V. R.} and Agafonov, {A. P.}",
note = "The work was financially supported by the Ministry of Science and Higher Education of the Russian Federation (Agreement no. 075-15-2021-1355 on December 10, 2021) within the implementation of individual events of the Federal Scientific and Technical Program for the Development of Synchrotron and Neutron Research and Research Infrastructure for 2019–2027. Публикация для корректировки.",
year = "2023",
month = dec,
doi = "10.1134/S1063774523601119",
language = "English",
volume = "68",
pages = "924--930",
journal = "Crystallography Reports",
issn = "1063-7745",
publisher = "PLEIADES PUBLISHING INC",
number = "6",

}

RIS

TY - JOUR

T1 - Preparation and Crystallization of Picornain 3C of Rhinovirus A28

AU - Tishin, A. E.

AU - Gladysheva, A. A.

AU - Pyatavina, L. A.

AU - Olkin, S. E.

AU - Gladysheva, A. A.

AU - Imatdionov, I. R.

AU - Vlaskina, A. V.

AU - Nikolaeva, A. Yu

AU - Samygina, V. R.

AU - Agafonov, A. P.

N1 - The work was financially supported by the Ministry of Science and Higher Education of the Russian Federation (Agreement no. 075-15-2021-1355 on December 10, 2021) within the implementation of individual events of the Federal Scientific and Technical Program for the Development of Synchrotron and Neutron Research and Research Infrastructure for 2019–2027. Публикация для корректировки.

PY - 2023/12

Y1 - 2023/12

N2 - Human rhinovirus picornain 3C is a high-value commercial cysteine protease, which is widely used to remove affinity tags and fusion proteins during the purification of the target proteins. A variant of rhinovirus A28 picornain 3C produced in this study is not annotated in the NCBI databases, shares 79% sequence identity in the PDB, and was not previously used in the protein engineering. A protocol was developed for the isolation and purification of the protein to use it in structural studies. The initial crystallization conditions were found. The determination and analysis of the structure of rhinovirus A28 picornain 3C will provide new possibilities for performing basic research on the evolution of proteolytic enzymes and for the design of the optimal variant of this protease.

AB - Human rhinovirus picornain 3C is a high-value commercial cysteine protease, which is widely used to remove affinity tags and fusion proteins during the purification of the target proteins. A variant of rhinovirus A28 picornain 3C produced in this study is not annotated in the NCBI databases, shares 79% sequence identity in the PDB, and was not previously used in the protein engineering. A protocol was developed for the isolation and purification of the protein to use it in structural studies. The initial crystallization conditions were found. The determination and analysis of the structure of rhinovirus A28 picornain 3C will provide new possibilities for performing basic research on the evolution of proteolytic enzymes and for the design of the optimal variant of this protease.

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85184150027&origin=inward&txGid=9a11e9f304adb0cc836b6d3818302f11

UR - https://www.mendeley.com/catalogue/1c1b3e67-b550-330f-b9ca-1e97fb99a84a/

U2 - 10.1134/S1063774523601119

DO - 10.1134/S1063774523601119

M3 - Article

VL - 68

SP - 924

EP - 930

JO - Crystallography Reports

JF - Crystallography Reports

SN - 1063-7745

IS - 6

ER -

ID: 59658975