|Entry||Database: EMDB / ID: 1634|
|Title||Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system.|
|Map data||This is a 3D map of a TatBC complex with one sufI substrate bound.|
|Sample||tatBC structure with one sufI substrate bound:|
twin arginine transporter
|Keywords||twin arginine / Tat / protein transport / blue native PAGE / single particle electron microscopy|
|Source||Escherichia coli (E. coli)|
|Method||single particle reconstruction / negative staining|
|Authors||Tarry MJ / Schaefer E / Chen S / Buchanan G / Greene NP / Lea SM / Palmer T / Saibil HR / Berks BC|
|Citation||Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2009|
Title: Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system.
Authors: Michael J Tarry / Eva Schäfer / Shuyun Chen / Grant Buchanan / Nicholas P Greene / Susan M Lea / Tracy Palmer / Helen R Saibil / Ben C Berks
|Date||Deposition: Jul 8, 2009 / Header (metadata) release: Jul 21, 2009 / Map release: Jul 21, 2009 / Last update: Oct 10, 2012|
|Structure viewer||EM map: |
Downloads & links
|File||emd_1634.map.gz (map file in CCP4 format, 1025 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 5 Å|
CCP4 map header:
-Entire tatBC structure with one sufI substrate bound
|Entire||Name: tatBC structure with one sufI substrate bound / Number of components: 3|
-Component #1: protein, twin arginine transporter
|Protein||Name: twin arginine transporter / a.k.a: tat / Recombinant expression: Yes|
|Source||Species: Escherichia coli (E. coli)|
|Specimen||Specimen state: particle / Method: negative staining|
|Sample solution||pH: 0.014|
|Staining||negatively stained with 2% (wt/vol) uranyl acetate on glow discharged, continuous carbon-coated 300 mesh copper grids (Agar Scientific).|
|Vitrification||Instrument: NONE / Cryogen name: NONE|
-Electron microscopy imaging
|Imaging||Microscope: FEI TECNAI 12|
|Electron gun||Electron source: TUNGSTEN HAIRPIN / Accelerating voltage: 120 kV / Illumination mode: OTHER|
|Lens||Magnification: 42000 X (nominal) / Imaging mode: BRIGHT FIELD / Defocus: 1500 - 2000 nm|
|Specimen Holder||Holder: eucentric / Model: OTHER / Tilt Angle: 0 - 50 deg.|
|Camera||Detector: KODAK SO-163 FILM|
|Image acquisition||Scanner: ZEISS SCAI / Sampling size: 7 microns|
Details: Micrographs were digitized on a Zeiss SCAI scanner at a pixel size of 7 micron, corresponding to 1.667 angstroms on the specimen. Subsequently, adjacent pixels were 3 x 3 averaged to yield a pixel size of 5 angstroms.
|Processing||Method: single particle reconstruction / Number of projections: 1556 / Applied symmetry: C1 (asymmetric)|
|3D reconstruction||Software: SPIDER|
Details: The tilted images were corrected for the effects of the contrast transfer function (CTF) by phase flipping, taking into account the defocus gradient across the micrographs and the position of each particle. Images were processed using SPIDER version 11.12 and 15.06. Three-dimensional reconstruction was performed by the random conical tilt method in SPIDER. The particles were windowed into 64 x 64 pixel boxes.
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