Design of an expression system to enhance MBP-mediated crystallization
Abstract
Crystallization chaperones have been used to facilitate the crystallization of challenging proteins. Even though the maltose-binding protein (MBP) is one of the most commonly used crystallization chaperones, the design of optimal expression constructs for crystallization of MBP fusion proteins remains a challenge. To increase the success rate of MBP-facilitated crystallization, a series of expression vectors have been designed with either a short flexible linker or a set of rigid helical linkers. Seven death domain superfamily members were tested for crystallization with this set of vectors, six of which had never been crystallized before. All of the seven targets were crystallized, and their structures were determined using at least one of the vectors. Our successful crystallization of all of the targets demonstrates the validity of our approach and expands the arsenal of the crystallization chaperone toolkit, which may be applicable to crystallization of other difficult protein targets, as well as to other crystallization chaperones.
- Authors:
-
- Univ. of Science and Technology of China, Hefei (China); National Inst. of Health (NIH), Bethesda, MD (United States)
- National Inst. of Health (NIH), Bethesda, MD (United States)
- Univ. of Science and Technology of China, Hefei (China)
- Case Western Reserve Univ., Cleveland, OH (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); National Cancer Inst.; National Inst. of General Medical Sciences; China Postdoctoral Science Foundation
- OSTI Identifier:
- 1357647
- Grant/Contract Number:
- AC02-98CH10886; Y1-CO-1020; Y1-GM-1104; 2015M582007
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Scientific Reports
- Additional Journal Information:
- Journal Volume: 7; Journal Issue: 1; Journal ID: ISSN 2045-2322
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; X-ray crystallography
Citation Formats
Jin, Tengchuan, Chuenchor, Watchalee, Jiang, Jiansheng, Cheng, Jinbo, Li, Yajuan, Fang, Kang, Huang, Mo, Smith, Patrick, and Xiao, Tsan Sam. Design of an expression system to enhance MBP-mediated crystallization. United States: N. p., 2017.
Web. doi:10.1038/srep40991.
Jin, Tengchuan, Chuenchor, Watchalee, Jiang, Jiansheng, Cheng, Jinbo, Li, Yajuan, Fang, Kang, Huang, Mo, Smith, Patrick, & Xiao, Tsan Sam. Design of an expression system to enhance MBP-mediated crystallization. United States. https://doi.org/10.1038/srep40991
Jin, Tengchuan, Chuenchor, Watchalee, Jiang, Jiansheng, Cheng, Jinbo, Li, Yajuan, Fang, Kang, Huang, Mo, Smith, Patrick, and Xiao, Tsan Sam. Mon .
"Design of an expression system to enhance MBP-mediated crystallization". United States. https://doi.org/10.1038/srep40991. https://www.osti.gov/servlets/purl/1357647.
@article{osti_1357647,
title = {Design of an expression system to enhance MBP-mediated crystallization},
author = {Jin, Tengchuan and Chuenchor, Watchalee and Jiang, Jiansheng and Cheng, Jinbo and Li, Yajuan and Fang, Kang and Huang, Mo and Smith, Patrick and Xiao, Tsan Sam},
abstractNote = {Crystallization chaperones have been used to facilitate the crystallization of challenging proteins. Even though the maltose-binding protein (MBP) is one of the most commonly used crystallization chaperones, the design of optimal expression constructs for crystallization of MBP fusion proteins remains a challenge. To increase the success rate of MBP-facilitated crystallization, a series of expression vectors have been designed with either a short flexible linker or a set of rigid helical linkers. Seven death domain superfamily members were tested for crystallization with this set of vectors, six of which had never been crystallized before. All of the seven targets were crystallized, and their structures were determined using at least one of the vectors. Our successful crystallization of all of the targets demonstrates the validity of our approach and expands the arsenal of the crystallization chaperone toolkit, which may be applicable to crystallization of other difficult protein targets, as well as to other crystallization chaperones.},
doi = {10.1038/srep40991},
journal = {Scientific Reports},
number = 1,
volume = 7,
place = {United States},
year = {Mon Jan 23 00:00:00 EST 2017},
month = {Mon Jan 23 00:00:00 EST 2017}
}
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Polymer-driven crystallization
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GPCR Engineering Yields High-Resolution Structural Insights into 2-Adrenergic Receptor Function
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Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain
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