|Entry||Database: EMDB / ID: 4443|
|Title||Structure of left-handed protein cage consisting of 24 eleven-membered ring proteins held together by gold (I) bridges.|
|Map data||map of the left-handed protein cage|
|Sample||Designed protein cage consisting of C11-symmetric TRAP proteins coordinated by Au+1 ionsDesign:|
Transcription attenuation protein MtrB / ligand
|Function / homology||Transcription attenuation protein MtrB / Tryptophan RNA-binding attenuator protein-like domain superfamily / Tryptophan RNA-binding attenuator protein domain / Tryptophan RNA-binding attenuator protein / DNA-templated transcription, termination / regulation of transcription, DNA-templated / RNA binding / identical protein binding / Transcription attenuation protein MtrB|
Function and homology information
|Source||Geobacillus stearothermophilus (bacteria)|
|Method||single particle reconstruction / cryo EM / 3.7 Å resolution|
|Authors||Malay AD / Miyazaki N / Biela AP / Iwasaki K / Heddle JG|
|Citation||Journal: To Be Published|
Title: Structure of left-handed protein cage consisting of 24 eleven-membered ring proteins held together by gold (I) bridges.
Authors: Malay AD / Miyazaki N / Biela AP / Iwasaki K / Heddle JG
|Validation Report||PDB-ID: 6ib3|
SummaryFull reportAbout validation report
|Date||Deposition: Nov 28, 2018 / Header (metadata) release: Mar 6, 2019 / Map release: Mar 6, 2019 / Last update: Mar 6, 2019|
|Structure viewer||EM map: |
Downloads & links
|File||emd_4443.map.gz (map file in CCP4 format, 42593 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.74 Å|
CCP4 map header:
-Entire Designed protein cage consisting of C11-symmetric TRAP proteins c...
|Entire||Name: Designed protein cage consisting of C11-symmetric TRAP proteins coordinated by Au+1 ions|
Number of components: 3
-Component #1: protein, Designed protein cage consisting of C11-symmetric TRAP p...
|Protein||Name: Designed protein cage consisting of C11-symmetric TRAP proteins coordinated by Au+1 ionsDesign|
Recombinant expression: No
|Mass||Experimental: 2.2 MDa|
|Source||Species: Geobacillus stearothermophilus (bacteria)|
|Source (engineered)||Expression System: Escherichia coli (E. coli) / Vector: pET21b / Strain: BL21(DE3)|
-Component #2: protein, Transcription attenuation protein MtrB
|Protein||Name: Transcription attenuation protein MtrB / Number of Copies: 264 / Recombinant expression: No|
|Mass||Theoretical: 8.161224 kDa|
|Source||Species: Geobacillus stearothermophilus (bacteria)|
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
-Component #3: ligand, GOLD ION
|Ligand||Name: GOLD ION / Number of Copies: 120 / Recombinant expression: No|
|Mass||Theoretical: 0.196967 kDa|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Specimen conc.: 0.89 mg/ml / pH: 8|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 277 K / Humidity: 100 % / Details: 3.0 s blotting time.|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 4 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 176463|
|3D reconstruction||Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
|Modeling #1||Target criteria: gradient-driven minimization of combined map and restraints target|
Refinement space: REAL
Input PDB model: 4V4F, 4V4F, 4V4F, 4V4F, 4V4F, 4V4F, 4V4F, 4V4F, 4V4F, 4V4F, 4V4F
Chain ID: AA, AB, AC, AD, AE, AF, AG, AH, AI, AJ, AK
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