English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Expression, crystallization and preliminary X-ray crystallographic studies of the outer membrane protein OmpW from Escherichia coli.

Albrecht, R., Zeth, K., Söding, J., Lupas, A., & Linke, D. (2006). Expression, crystallization and preliminary X-ray crystallographic studies of the outer membrane protein OmpW from Escherichia coli. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(4), 415-418. doi:10.1107/S1744309106010190.

Item is

Files

show Files
hide Files
:
1944247.pdf (Publisher version), 611KB
Name:
1944247.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Albrecht, R.1, Author
Zeth, K.1, Author
Söding, J.2, Author           
Lupas, A.1, Author
Linke, D.1, Author
Affiliations:
1external, ou_persistent22              
2Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1933286              

Content

show
hide
Free keywords: OmpW; membrane proteins; outer membrane; homology modelling.
 Abstract: OmpW is an eight-stranded 21 kDa molecular-weight β-barrel protein from the outer membrane of Gram-negative bacteria. It is a major antigen in bacterial infections and has implications in antibiotic resistance and in the oxidative degradation of organic compounds. OmpW from Escherichia coli was cloned and the protein was expressed in inclusion bodies. A method for refolding and purification was developed which yields properly folded protein according to circular-dichroism measurements. The protein has been crystallized and crystals were obtained that diffracted to a resolution limit of 3.5 Å. The crystals belong to space group P422, with unit-cell parameters a = 122.5, c = 105.7 Å. A homology model of OmpW is presented based on known structures of eight-stranded β-barrels, intended for use in molecular-replacement trials.

Details

show
hide
Language(s): eng - English
 Dates: 2006-04-062006-04
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S1744309106010190
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Blackwell Publishing Limited
Pages: - Volume / Issue: 62 (4) Sequence Number: - Start / End Page: 415 - 418 Identifier: ISSN: 1744-3091
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017210_1