Three-dimensional structure of cytochrome c nitrite reductase as determined by cryo-electron microscopy

Standard

Three-dimensional structure of cytochrome c nitrite reductase as determined by cryo-electron microscopy. / Baymukhametov, T. N.; Chesnokov, Y. M.; Pichkur, E. B.; Boyko, K. M.; Tikhonova, T. V.; Myasnikov, A. G.; Vasiliev, A. L.; Lipkin, A. V.; Popov, V. O.; Kovalchuk, M. V.

в: Acta Naturae, Том 10, № 3, 2018, стр. 48-56.

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

Harvard

Baymukhametov, TN, Chesnokov, YM, Pichkur, EB, Boyko, KM, Tikhonova, TV, Myasnikov, AG, Vasiliev, AL, Lipkin, AV, Popov, VO & Kovalchuk, MV 2018, 'Three-dimensional structure of cytochrome c nitrite reductase as determined by cryo-electron microscopy', Acta Naturae, Том. 10, № 3, стр. 48-56. https://doi.org/10.32607/20758251-2018-10-3-48-56

APA

Baymukhametov, T. N., Chesnokov, Y. M., Pichkur, E. B., Boyko, K. M., Tikhonova, T. V., Myasnikov, A. G., Vasiliev, A. L., Lipkin, A. V., Popov, V. O., & Kovalchuk, M. V. (2018). Three-dimensional structure of cytochrome c nitrite reductase as determined by cryo-electron microscopy. Acta Naturae, 10(3), 48-56. https://doi.org/10.32607/20758251-2018-10-3-48-56

Vancouver

Baymukhametov TN, Chesnokov YM, Pichkur EB, Boyko KM, Tikhonova TV, Myasnikov AG и пр. Three-dimensional structure of cytochrome c nitrite reductase as determined by cryo-electron microscopy. Acta Naturae. 2018;10(3):48-56. https://doi.org/10.32607/20758251-2018-10-3-48-56

Author

Baymukhametov, T. N. ; Chesnokov, Y. M. ; Pichkur, E. B. ; Boyko, K. M. ; Tikhonova, T. V. ; Myasnikov, A. G. ; Vasiliev, A. L. ; Lipkin, A. V. ; Popov, V. O. ; Kovalchuk, M. V. / Three-dimensional structure of cytochrome c nitrite reductase as determined by cryo-electron microscopy. в: Acta Naturae. 2018 ; Том 10, № 3. стр. 48-56.

BibTeX

@article{249151f6a41a4dbcb0708d34d2029ed6,

title = "Three-dimensional structure of cytochrome c nitrite reductase as determined by cryo-electron microscopy",

abstract = "The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 {\AA} resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone and side-chain orientations in the cryo-EM-based model are, in general, similar to those in the high-resolution X-ray diffraction structure of this enzyme.",

keywords = "Cytochrome c nitrite reductase, High-resolution cryo-electron microscopy, Single particle analysis, Structural biology",

author = "Baymukhametov, {T. N.} and Chesnokov, {Y. M.} and Pichkur, {E. B.} and Boyko, {K. M.} and Tikhonova, {T. V.} and Myasnikov, {A. G.} and Vasiliev, {A. L.} and Lipkin, {A. V.} and Popov, {V. O.} and Kovalchuk, {M. V.}",

note = "Publisher Copyright: {\textcopyright} 2018 Park-media, Ltd.",

year = "2018",

doi = "10.32607/20758251-2018-10-3-48-56",

language = "English",

volume = "10",

pages = "48--56",

journal = "Acta Naturae",

issn = "2075-8251",

publisher = "Парк-медиа",

number = "3",

}

RIS

TY - JOUR

T1 - Three-dimensional structure of cytochrome c nitrite reductase as determined by cryo-electron microscopy

AU - Baymukhametov, T. N.

AU - Chesnokov, Y. M.

AU - Pichkur, E. B.

AU - Boyko, K. M.

AU - Tikhonova, T. V.

AU - Myasnikov, A. G.

AU - Vasiliev, A. L.

AU - Lipkin, A. V.

AU - Popov, V. O.

AU - Kovalchuk, M. V.

PY - 2018

Y1 - 2018

N2 - The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 Å resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone and side-chain orientations in the cryo-EM-based model are, in general, similar to those in the high-resolution X-ray diffraction structure of this enzyme.

AB - The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 Å resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone and side-chain orientations in the cryo-EM-based model are, in general, similar to those in the high-resolution X-ray diffraction structure of this enzyme.

KW - Cytochrome c nitrite reductase

KW - High-resolution cryo-electron microscopy

KW - Single particle analysis

KW - Structural biology

UR - http://www.scopus.com/inward/record.url?scp=85062937227&partnerID=8YFLogxK

U2 - 10.32607/20758251-2018-10-3-48-56

DO - 10.32607/20758251-2018-10-3-48-56

M3 - Article

AN - SCOPUS:85062937227

VL - 10

SP - 48

EP - 56

JO - Acta Naturae

JF - Acta Naturae

SN - 2075-8251

IS - 3

ER -

ID: 88199000