MIT Libraries logoDSpace@MIT

MIT
View Item 
  • DSpace@MIT Home
  • MIT Open Access Articles
  • MIT Open Access Articles
  • View Item
  • DSpace@MIT Home
  • MIT Open Access Articles
  • MIT Open Access Articles
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Optimized E.coli expression strain LOBSTR eliminates common contaminants from His-tag purification

Author(s)
Andersen, Kasper R.; Leksa, Nina Carolina; Schwartz, Thomas
Thumbnail
DownloadSchwartz_Optimized e.coli.pdf (612.9Kb)
OPEN_ACCESS_POLICY

Open Access Policy

Creative Commons Attribution-Noncommercial-Share Alike

Terms of use
Creative Commons Attribution-Noncommercial-Share Alike http://creativecommons.org/licenses/by-nc-sa/4.0/
Metadata
Show full item record
Abstract
His-tag affinity purification is one of the most commonly used methods to purify recombinant proteins expressed in E. coli. One drawback of using the His-tag is the co-purification of contaminating histidine-rich E. coli proteins. We engineered a new E. coli expression strain, LOBSTR (low background strain), which eliminates the most abundant contaminants. LOBSTR is derived from the E. coli BL21(DE3) strain and carries genomically modified copies of arnA and slyD, whose protein products exhibit reduced affinities to Ni and Co resins, resulting in a much higher purity of the target protein. The use of LOBSTR enables the pursuit of challenging low-expressing protein targets by reducing background contamination with no additional purification steps, materials, or costs, and thus pushes the limits of standard His-tag purifications.
Date issued
2013-08
URI
http://hdl.handle.net/1721.1/96797
Department
Massachusetts Institute of Technology. Department of Biology
Journal
Proteins: Structure, Function, and Bioinformatics
Publisher
Wiley Blackwell
Citation
Andersen, Kasper R., Nina C. Leksa, and Thomas U. Schwartz. “Optimized E. Coli Expression Strain LOBSTR Eliminates Common Contaminants from His-Tag Purification.” Proteins: Structure, Function, and Bioinformatics 81, no. 11 (August 23, 2013): 1857–1861.
Version: Author's final manuscript
ISSN
08873585
1097-0134

Collections
  • MIT Open Access Articles

Browse

All of DSpaceCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

My Account

Login

Statistics

OA StatisticsStatistics by CountryStatistics by Department
MIT Libraries
PrivacyPermissionsAccessibilityContact us
MIT
Content created by the MIT Libraries, CC BY-NC unless otherwise noted. Notify us about copyright concerns.