ArticleProtein science : a publication of the Protein Society2004
Design, expression, and purification of a Flaviviridae polymerase using a high-throughput approach to facilitate crystal structure determination.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Crystal Structure of Classical Swine Fever Virus NS5B Reveals a Novel N-Terminal Domain.Journal of virology · 2018Article
- A Structural Overview of RNA-Dependent RNA Polymerases from the Flaviviridae Family.International journal of molecular sciences · 2015Review
- Article
- The VIZIER project: overview; expectations; and achievements.Antiviral research · 2010Review
- The role of medical structural genomics in discovering new drugs for infectious diseases.PLoS computational biology · 2009Review
- Fragment-based cocktail crystallography by the medical structural genomics of pathogenic protozoa consortium.Current topics in medicinal chemistry · 2009Review
- Economical parallel protein expression screening and scale-up in Escherichia coli.Journal of structural and functional genomics · 2006Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
Abstract
Bovine viral diarrhea virus (BVDV) nonstructural protein 5B is an RNA-dependent RNA polymerase, essential for viral replication. Initial attempts to crystallize a soluble form of the 695-residue BVDV polymerase did not produce any crystals. Limited proteolysis, homology modeling, and mutagenesis data were used to aid the design of polymerase constructs that might crystallize more readily. Limited proteolysis of the polymerase with trypsin identified a domain boundary within the protein. Homology modeling of the polymerase, based on the structure of hepatitis C virus polymerase, indicated that the two polymerases share a 23% identical "core," although overall sequence identity is low. Eighty-four expression clones of the BVDV polymerase were designed by fine-sampling of chain termini at the boundaries of domain and of active truncated forms of the polymerase. The resulting constructs were expressed in Escherichia coli and purified using high-throughput methods. Soluble truncated proteins were subjected to crystallization trials in a 96-well format, and two of these proteins were successfully crystallized.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.