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Small-angle X-ray scattering study of conditions for the formation of growth units of protein crystals in lysozyme solutions. / Dyakova, Yu A.; Ilina, K. B.; Konarev, P. V.; Kryukova, A. E.; Marchenkova, M. A.; Blagov, A. E.; Volkov, V. V.; Pisarevsky, Yu V.; Kovalchuk, M. V.
в:
Crystallography Reports, Том 62, № 3, 01.05.2017, стр. 364-369.
Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Harvard
Dyakova, YA, Ilina, KB, Konarev, PV, Kryukova, AE, Marchenkova, MA, Blagov, AE, Volkov, VV, Pisarevsky, YV
& Kovalchuk, MV 2017, '
Small-angle X-ray scattering study of conditions for the formation of growth units of protein crystals in lysozyme solutions',
Crystallography Reports, Том. 62, № 3, стр. 364-369.
https://doi.org/10.1134/S1063774517030051APA
Dyakova, Y. A., Ilina, K. B., Konarev, P. V., Kryukova, A. E., Marchenkova, M. A., Blagov, A. E., Volkov, V. V., Pisarevsky, Y. V.
, & Kovalchuk, M. V. (2017).
Small-angle X-ray scattering study of conditions for the formation of growth units of protein crystals in lysozyme solutions.
Crystallography Reports,
62(3), 364-369.
https://doi.org/10.1134/S1063774517030051Vancouver
Author
Dyakova, Yu A. ; Ilina, K. B. ; Konarev, P. V. ; Kryukova, A. E. ; Marchenkova, M. A. ; Blagov, A. E. ; Volkov, V. V. ; Pisarevsky, Yu V.
; Kovalchuk, M. V. /
Small-angle X-ray scattering study of conditions for the formation of growth units of protein crystals in lysozyme solutions. в:
Crystallography Reports. 2017 ; Том 62, № 3. стр. 364-369.
BibTeX
@article{ae1b33c3dee8460a89a378ef93dca1c9,
title = "Small-angle X-ray scattering study of conditions for the formation of growth units of protein crystals in lysozyme solutions",
abstract = "The structural composition of lysozyme solutions favorable for the formation of the tetragonal form of protein crystals was studied by synchrotron-based small-angle X-ray scattering depending on the protein concentration and the temperature. Along with lysozyme monomers, dimers and octamers are found in crystallization solutions; the octamer content increases with an increase in the protein concentration.",
author = "Dyakova, {Yu A.} and Ilina, {K. B.} and Konarev, {P. V.} and Kryukova, {A. E.} and Marchenkova, {M. A.} and Blagov, {A. E.} and Volkov, {V. V.} and Pisarevsky, {Yu V.} and Kovalchuk, {M. V.}",
note = "Publisher Copyright: {\textcopyright} 2017, Pleiades Publishing, Inc.",
year = "2017",
month = may,
day = "1",
doi = "10.1134/S1063774517030051",
language = "English",
volume = "62",
pages = "364--369",
journal = "Crystallography Reports",
issn = "1063-7745",
publisher = "МАИК {"}Наука/Интерпериодика{"}",
number = "3",
}
RIS
TY - JOUR
T1 - Small-angle X-ray scattering study of conditions for the formation of growth units of protein crystals in lysozyme solutions
AU - Dyakova, Yu A.
AU - Ilina, K. B.
AU - Konarev, P. V.
AU - Kryukova, A. E.
AU - Marchenkova, M. A.
AU - Blagov, A. E.
AU - Volkov, V. V.
AU - Pisarevsky, Yu V.
AU - Kovalchuk, M. V.
N1 - Publisher Copyright:
© 2017, Pleiades Publishing, Inc.
PY - 2017/5/1
Y1 - 2017/5/1
N2 - The structural composition of lysozyme solutions favorable for the formation of the tetragonal form of protein crystals was studied by synchrotron-based small-angle X-ray scattering depending on the protein concentration and the temperature. Along with lysozyme monomers, dimers and octamers are found in crystallization solutions; the octamer content increases with an increase in the protein concentration.
AB - The structural composition of lysozyme solutions favorable for the formation of the tetragonal form of protein crystals was studied by synchrotron-based small-angle X-ray scattering depending on the protein concentration and the temperature. Along with lysozyme monomers, dimers and octamers are found in crystallization solutions; the octamer content increases with an increase in the protein concentration.
UR - http://www.scopus.com/inward/record.url?scp=85020415736&partnerID=8YFLogxK
U2 - 10.1134/S1063774517030051
DO - 10.1134/S1063774517030051
M3 - Article
AN - SCOPUS:85020415736
VL - 62
SP - 364
EP - 369
JO - Crystallography Reports
JF - Crystallography Reports
SN - 1063-7745
IS - 3
ER -
