Nature of impurities during protein crystallization

Standard

Nature of impurities during protein crystallization. / Baskakova, S. S.; Volkov, V. V.; Laptinskaya, T. V.; Lyasnikova, M. S.; Voloshin, A. E.; Koval’chuk, M. V.

In: Crystallography Reports, Vol. 62, No. 1, 01.01.2017, p. 148-156.

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

Harvard

Baskakova, SS, Volkov, VV, Laptinskaya, TV, Lyasnikova, MS, Voloshin, AE & Koval’chuk, MV 2017, 'Nature of impurities during protein crystallization', Crystallography Reports, vol. 62, no. 1, pp. 148-156. https://doi.org/10.1134/S1063774517010060

APA

Baskakova, S. S., Volkov, V. V., Laptinskaya, T. V., Lyasnikova, M. S., Voloshin, A. E., & Koval’chuk, M. V. (2017). Nature of impurities during protein crystallization. Crystallography Reports, 62(1), 148-156. https://doi.org/10.1134/S1063774517010060

Vancouver

Baskakova SS, Volkov VV, Laptinskaya TV, Lyasnikova MS, Voloshin AE, Koval’chuk MV. Nature of impurities during protein crystallization. Crystallography Reports. 2017 Jan 1;62(1):148-156. https://doi.org/10.1134/S1063774517010060

Author

Baskakova, S. S. ; Volkov, V. V. ; Laptinskaya, T. V. ; Lyasnikova, M. S. ; Voloshin, A. E. ; Koval’chuk, M. V. / Nature of impurities during protein crystallization. In: Crystallography Reports. 2017 ; Vol. 62, No. 1. pp. 148-156.

BibTeX

@article{0dc00d640bd2492da1e131a2d11ec7ae,

title = "Nature of impurities during protein crystallization",

abstract = "Lysozyme crystal growth was studied using reagents of different purity of three trademarks— Seikagaku Corporation (sixfold recrystallized lysozyme), Sigma-Aldrich (threefold recrystallized lysozyme), and Hampton Research (threefold recrystallized lysozyme). Solutions of these reagents were investigated by small-angle X-ray scattering, dynamic light scattering (DLS), ultracentrifugation, and electrophoresis. It was found that crystal-growth and oligomerization processes are more intense in solutions of the reagent of higher purity. The dependences of the fraction of lysozyme oligomers on the supersaturation and purity of the solution are analyzed.",

author = "Baskakova, {S. S.} and Volkov, {V. V.} and Laptinskaya, {T. V.} and Lyasnikova, {M. S.} and Voloshin, {A. E.} and Koval{\textquoteright}chuk, {M. V.}",

note = "Publisher Copyright: {\textcopyright} 2017, Pleiades Publishing, Inc.",

year = "2017",

month = jan,

day = "1",

doi = "10.1134/S1063774517010060",

language = "English",

volume = "62",

pages = "148--156",

journal = "Crystallography Reports",

issn = "1063-7745",

publisher = "МАИК {"}Наука/Интерпериодика{"}",

number = "1",

}

RIS

TY - JOUR

T1 - Nature of impurities during protein crystallization

AU - Baskakova, S. S.

AU - Volkov, V. V.

AU - Laptinskaya, T. V.

AU - Lyasnikova, M. S.

AU - Voloshin, A. E.

AU - Koval’chuk, M. V.

PY - 2017/1/1

Y1 - 2017/1/1

N2 - Lysozyme crystal growth was studied using reagents of different purity of three trademarks— Seikagaku Corporation (sixfold recrystallized lysozyme), Sigma-Aldrich (threefold recrystallized lysozyme), and Hampton Research (threefold recrystallized lysozyme). Solutions of these reagents were investigated by small-angle X-ray scattering, dynamic light scattering (DLS), ultracentrifugation, and electrophoresis. It was found that crystal-growth and oligomerization processes are more intense in solutions of the reagent of higher purity. The dependences of the fraction of lysozyme oligomers on the supersaturation and purity of the solution are analyzed.

AB - Lysozyme crystal growth was studied using reagents of different purity of three trademarks— Seikagaku Corporation (sixfold recrystallized lysozyme), Sigma-Aldrich (threefold recrystallized lysozyme), and Hampton Research (threefold recrystallized lysozyme). Solutions of these reagents were investigated by small-angle X-ray scattering, dynamic light scattering (DLS), ultracentrifugation, and electrophoresis. It was found that crystal-growth and oligomerization processes are more intense in solutions of the reagent of higher purity. The dependences of the fraction of lysozyme oligomers on the supersaturation and purity of the solution are analyzed.

UR - http://www.scopus.com/inward/record.url?scp=85013679084&partnerID=8YFLogxK

U2 - 10.1134/S1063774517010060

DO - 10.1134/S1063774517010060

M3 - Article

AN - SCOPUS:85013679084

VL - 62

SP - 148

EP - 156

JO - Crystallography Reports

JF - Crystallography Reports

SN - 1063-7745

IS - 1

ER -

ID: 88202638