Nature of impurities during protein crystallization


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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.

作者简介

S. Baskakova

Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics”

编辑信件的主要联系方式.
Email: SvetlBaskakova@yandex.ru
俄罗斯联邦, Moscow, 119333

V. Volkov

Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics”

Email: SvetlBaskakova@yandex.ru
俄罗斯联邦, Moscow, 119333

T. Laptinskaya

Moscow State University

Email: SvetlBaskakova@yandex.ru
俄罗斯联邦, Moscow, 119992

M. Lyasnikova

Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics”

Email: SvetlBaskakova@yandex.ru
俄罗斯联邦, Moscow, 119333

A. Voloshin

Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics”

Email: SvetlBaskakova@yandex.ru
俄罗斯联邦, Moscow, 119333

M. Koval’chuk

Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics”; National Research Centre “Kurchatov Institute,”

Email: SvetlBaskakova@yandex.ru
俄罗斯联邦, Moscow, 119333; Moscow, 123098

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