ID 112469
著者
津下, 英明 Kyoto Sangyo University
Hondoh, Hironori Hiroshima University
Uehara, Yuta Tokushima University
Hosokawa, Kohei Tokushima University
キーワード
precipitant-free
lysozyme
centrifugal concentration
synchrotron x-ray crystallography
資料タイプ
学術雑誌論文
抄録
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.
掲載誌名
Crystal Growth & Design
ISSN
15287483
15287505
cat書誌ID
AA1150352X
AA12478723
出版者
ACS Publications
18
8
開始ページ
4226
終了ページ
4229
発行日
2018-07-13
備考
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
権利情報
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.
EDB ID
出版社版DOI
出版社版URL
フルテキストファイル
言語
eng
著者版フラグ
著者版
部局
理工学系
先端酵素学研究所
技術支援部