5H7N

Crystal structure of human NLRP12-PYD with a MBP tag

Summary for 5H7N

• Entry DOI: 10.2210/pdb5h7n/pdb
• Related: 5H7Q
• Related PRD ID: PRD_900010
• Descriptor: NLRP12-PYD with MBP tag, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (6 entities in total)
• Functional Keywords: maltose binding protein, crystallization tag, death fold, sugar binding protein
• Biological source: Homo sapiens
• Total number of polymer chains: 2
• Total formula weight: 107405.18

Authors

Jin, T.C.,Xiao, T.S. (deposition date: 2016-11-19, release date: 2017-02-15, Last modification date: 2023-11-08)

Primary citation

Jin, T.C.,Chuenchor, W.,Jiang, J.,Cheng, J.,Li, Y.,Fang, K.,Huang, M.,Smith, P.,Xiao, T.S.
Design of an expression system to enhance MBP-mediated crystallization
Sci Rep, 7:40991-40991, 2017

PubMed 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.

PubMed: 28112203
DOI: 10.1038/srep40991

Experimental method

X-RAY DIFFRACTION (1.849 Å)