ArticleScientific reports2017
Design of an expression system to enhance MBP-mediated crystallization.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 56 citations in OpenAlex.
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- Death domain fold proteins in immune signaling and transcriptional regulation.The FEBS journal · 2022Review
- Directionality of PYD filament growth determined by the transition of NLRP3 nucleation seeds to ASC elongation.Science advances · 2022Article
- Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex.Scientific reports · 2021Article
- Molecular mechanism for vitamin C-derived CNature communications · 2021Article
- Homotypic CARD-CARD interaction is critical for the activation of NLRP1 inflammasome.Cell death & disease · 2021Article
- Structure of High-Risk Papillomavirus 31 E6 Oncogenic Protein and Characterization of E6/E6AP/p53 Complex Formation.Journal of virology · 2020Article
- High-resolution crystal structure and biochemical characterization of a GH11 endoxylanase from Nectria haematococca.Scientific reports · 2020Article
- Crystal structure of caspase-11 CARD provides insights into caspase-11 activation.Cell discovery · 2020Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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