Standard

In situ study of the state of lysozyme molecules at the very early stage of the crystallization process by small-angle X-ray scattering. / Marchenkova, M. A.; Volkov, V. V.; Blagov, A. E.; Dyakova, Yu A.; Ilina, K. B.; Tereschenko, E. Yu; Timofeev, V. I.; Pisarevsky, Yu V.; Kovalchuk, M. V.

In: Crystallography Reports, Vol. 61, No. 1, 01.01.2016, p. 5-10.

Research output: Contribution to journal › Article › peer-review

Harvard

Marchenkova, MA, Volkov, VV, Blagov, AE, Dyakova, YA, Ilina, KB, Tereschenko, EY, Timofeev, VI, Pisarevsky, YV & Kovalchuk, MV 2016, 'In situ study of the state of lysozyme molecules at the very early stage of the crystallization process by small-angle X-ray scattering', Crystallography Reports, vol. 61, no. 1, pp. 5-10. https://doi.org/10.1134/S1063774516010144

APA

Marchenkova, M. A., Volkov, V. V., Blagov, A. E., Dyakova, Y. A., Ilina, K. B., Tereschenko, E. Y., Timofeev, V. I., Pisarevsky, Y. V., & Kovalchuk, M. V. (2016). In situ study of the state of lysozyme molecules at the very early stage of the crystallization process by small-angle X-ray scattering. Crystallography Reports, 61(1), 5-10. https://doi.org/10.1134/S1063774516010144

Vancouver

Marchenkova MA, Volkov VV, Blagov AE, Dyakova YA, Ilina KB, Tereschenko EY et al. In situ study of the state of lysozyme molecules at the very early stage of the crystallization process by small-angle X-ray scattering. Crystallography Reports. 2016 Jan 1;61(1):5-10. https://doi.org/10.1134/S1063774516010144

Author

Marchenkova, M. A. ; Volkov, V. V. ; Blagov, A. E. ; Dyakova, Yu A. ; Ilina, K. B. ; Tereschenko, E. Yu ; Timofeev, V. I. ; Pisarevsky, Yu V. ; Kovalchuk, M. V. / In situ study of the state of lysozyme molecules at the very early stage of the crystallization process by small-angle X-ray scattering. In: Crystallography Reports. 2016 ; Vol. 61, No. 1. pp. 5-10.

BibTeX

@article{e91c61729e074360bb6905b31819c13a,
title = "In situ study of the state of lysozyme molecules at the very early stage of the crystallization process by small-angle X-ray scattering",
abstract = "The molecular state of hen egg white lysozyme in solution has been studied by small-angle X-ray scattering (SAXS) combined with molecular simulation. The addition of a precipitant is shown to change the state of the protein molecules in solution. The SAXS data were processed using the constructed models of different oligomers. Under the crystallization conditions, lysozyme is shown to be present in solution as monomers (96.0%), dimers (1.9%), and octamers (2.1%), whereas tetramers and hexamers are not found. The modeled structure of the octamer is not consistent with the commonly accepted unit cell containing eight lysozyme molecules. Meanwhile, the modeled octamers are well-fitted to the crystal structure and can serve as building blocks in the course of crystal growth.",
author = "Marchenkova, {M. A.} and Volkov, {V. V.} and Blagov, {A. E.} and Dyakova, {Yu A.} and Ilina, {K. B.} and Tereschenko, {E. Yu} and Timofeev, {V. I.} and Pisarevsky, {Yu V.} and Kovalchuk, {M. V.}",
note = "Publisher Copyright: {\textcopyright} 2016, Pleiades Publishing, Inc.",
year = "2016",
month = jan,
day = "1",
doi = "10.1134/S1063774516010144",
language = "English",
volume = "61",
pages = "5--10",
journal = "Crystallography Reports",
issn = "1063-7745",
publisher = "МАИК {"}Наука/Интерпериодика{"}",
number = "1",

}

RIS

TY - JOUR

T1 - In situ study of the state of lysozyme molecules at the very early stage of the crystallization process by small-angle X-ray scattering

AU - Marchenkova, M. A.

AU - Volkov, V. V.

AU - Blagov, A. E.

AU - Dyakova, Yu A.

AU - Ilina, K. B.

AU - Tereschenko, E. Yu

AU - Timofeev, V. I.

AU - Pisarevsky, Yu V.

AU - Kovalchuk, M. V.

N1 - Publisher Copyright: © 2016, Pleiades Publishing, Inc.

PY - 2016/1/1

Y1 - 2016/1/1

N2 - The molecular state of hen egg white lysozyme in solution has been studied by small-angle X-ray scattering (SAXS) combined with molecular simulation. The addition of a precipitant is shown to change the state of the protein molecules in solution. The SAXS data were processed using the constructed models of different oligomers. Under the crystallization conditions, lysozyme is shown to be present in solution as monomers (96.0%), dimers (1.9%), and octamers (2.1%), whereas tetramers and hexamers are not found. The modeled structure of the octamer is not consistent with the commonly accepted unit cell containing eight lysozyme molecules. Meanwhile, the modeled octamers are well-fitted to the crystal structure and can serve as building blocks in the course of crystal growth.

AB - The molecular state of hen egg white lysozyme in solution has been studied by small-angle X-ray scattering (SAXS) combined with molecular simulation. The addition of a precipitant is shown to change the state of the protein molecules in solution. The SAXS data were processed using the constructed models of different oligomers. Under the crystallization conditions, lysozyme is shown to be present in solution as monomers (96.0%), dimers (1.9%), and octamers (2.1%), whereas tetramers and hexamers are not found. The modeled structure of the octamer is not consistent with the commonly accepted unit cell containing eight lysozyme molecules. Meanwhile, the modeled octamers are well-fitted to the crystal structure and can serve as building blocks in the course of crystal growth.

UR - http://www.scopus.com/inward/record.url?scp=84955584284&partnerID=8YFLogxK

U2 - 10.1134/S1063774516010144

DO - 10.1134/S1063774516010144

M3 - Article

AN - SCOPUS:84955584284

VL - 61

SP - 5

EP - 10

JO - Crystallography Reports

JF - Crystallography Reports

SN - 1063-7745

IS - 1

ER -

ID: 88204921