English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Purification, crystallization and preliminary X-ray diffraction analysis of the FeoB G domain from Methanococcus jannaschii

Köster, S., Kühlbrandt, W., & Yildiz, Ö. (2009). Purification, crystallization and preliminary X-ray diffraction analysis of the FeoB G domain from Methanococcus jannaschii. Acta Crystallographie Section F Structural Biology and Crystallization Communications, F65(7), 684-687. doi:10.1107/S1744309109019216.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Köster, Stefan1, Author           
Kühlbrandt, Werner1, Author                 
Yildiz, Özkan1, Author                 
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

Content

show
hide
Free keywords: FeoB; G domains; Methanococcus jannaschii; membrane proteins
 Abstract: The transmembrane protein FeoB plays a key role in ferrous iron acquisition in prokaryotes. The N-terminal domain of FeoB from Methanococcus jannaschii was overproduced, purified to homogeneity and crystallized in the presence of GTP and magnesium. The native protein crystallized in a tetragonal space group and the crystals diffracted to beyond 2.2 Å resolution, with unit-cell parameters a = b = 84.77, c = 137.90 Å. The Matthews coefficient and the solvent content were estimated to be 2.65 Å3 Da-1 and 53.64%, respectively, which corresponds to the presence of two molecules per asymmetric unit. To obtain initial phases, selenomethionyl-substituted protein was overproduced, purified and crystallized

Details

show
hide
Language(s): eng - English
 Dates: 2009-06-272009-07-01
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S1744309109019216
PMID: 19574639
PMC: PMC2705634
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Acta Crystallographie Section F Structural Biology and Crystallization Communications
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Blackwell Publishing Limited
Pages: - Volume / Issue: F65 (7) Sequence Number: - Start / End Page: 684 - 687 Identifier: ISSN: 1744-3091
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017210_2