ID 112910
Author
Content Type
Journal Article
Description
The protein crystallization process requires screening a large number of conditions using a large quantity of high-purity protein, which makes crystal structure analysis difficult. Thus, the development of easy and versatile protein crystallization techniques is both extremely desirable and highly challenging. Here, I demonstrate the crystallization and structure determination of ubiquitin by genetic fusion to the highly porous honeycomb lattice of R1EN. I successfully crystallized and collected X-ray data from three R1EN-ubiquitin constructs with varied linker lengths under the same conditions as the original R1EN. The crystals diffracted to 1.7-2.4 Å resolution, and the ubiquitin structures were determined with results almost identical to the previously published structure. Moreover, the ubiquitin structure could be solved by molecular replacement using R1EN alone. This method may reduce the effort required for crystallization screening and is applicable to de novo protein structure determination.
Journal Title
Journal of the American Chemical Society
ISSN
00027863
15205126
NCID
AA00692602
AA12097173
Publisher
American Chemical Society
Volume
140
Issue
42
Start Page
13546
End Page
13549
Published Date
2018-10-09
Remark
論文本文は2019-10-09以降公開予定
Rights
This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher.
EDB ID
DOI (Published Version)
URL ( Publisher's Version )
language
eng
TextVersion
その他
departments
Institute of Advanced Medical Sciences