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ID 112469
Author
Tsuge, Hideaki Kyoto Sangyo University
Hondoh, Hironori Hiroshima University
Kato, Yusuke Tokushima Bunri University KAKEN Search Researchers
Uehara, Yuta Tokushima University
Hosokawa, Kohei Tokushima University
Keywords
precipitant-free
lysozyme
centrifugal concentration
synchrotron x-ray crystallography
Content Type
Journal Article
Description
The three-dimensional (3D) structure of a protein molecule in its crystal need not correspond to that found in vivo in many cases, since we usually crystallize protein molecules using precipitants (salts, organic solvents, polymeric electrolytes, etc.), and the precipitants are often incorporated into crystals along with the protein molecules. Although precipitant-free crystallization methods would solve these problems, such methods had not yet been established. We have achieved a novel precipitant-free crystallization method by liquid-liquid phase separation during the centrifugal concentration of lysozyme in ultra-pure water. In the 3D structure of the precipitant-free crystal, lysozyme loses a sodium cation and changes the position of Ser 72. Deionization of the solution also appears to induce a change in the position of Asp 101 and an increase in the activity of lysozyme.
Journal Title
Crystal Growth & Design
ISSN
15287483
15287505
NCID
AA1150352X
AA12478723
Publisher
ACS Publications
Volume
18
Issue
8
Start Page
4226
End Page
4229
Published Date
2018-07-13
Remark
The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.cgd.8b00326.

・Materials and methods, an image of a precipitant-free GI crystal and its oscillation photograph, X-ray data collection statistics, and rough estimate of crystallization conditions (PDF) : cgd_18_8_4226_si.pdf
Rights
This document is the Accepted Manuscript version of a Published Work that appeared in final form in Crystal Growth & Design, copyright © American Chemical Society after peer review and technical editing by the publisher.
To access the final edited and published work see https://doi.org/10.1021/acs.cgd.8b00326.
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DOI (Published Version)
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
Author
departments
Science and Technology
Institute of Advanced Medical Sciences
Technical Support Department