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Yorodumi- PDB-8wpz: Cryo-ET structure of RuBisCO at 3.9 angstroms from Synechococcus ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8wpz | ||||||
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Title | Cryo-ET structure of RuBisCO at 3.9 angstroms from Synechococcus elongatus PCC 7942 | ||||||
Components |
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Keywords | PHOTOSYNTHESIS / carboxysome / RuBisCO / cryo-et | ||||||
Function / homology | Function and homology information carboxysome / photorespiration / ribulose-bisphosphate carboxylase / ribulose-bisphosphate carboxylase activity / reductive pentose-phosphate cycle / monooxygenase activity / magnesium ion binding Similarity search - Function | ||||||
Biological species | Synechococcus elongatus PCC 7942 = FACHB-805 (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 3.9 Å | ||||||
Authors | Kong, W.W. / Jiang, Y.L. / Zhou, C.Z. | ||||||
Funding support | China, 1items
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Citation | Journal: To Be Published Title: Cryo-electron tomography reveals the packaging pattern of RuBisCOs in Synechococcus beta-carboxysome Authors: Kong, W.W. / Zhu, Y. / Zhao, H.R. / Du, K. / Zhou, R.Q. / Li, B. / Yang, F. / Hou, P. / Chen, Y. / Sun, F. / Jiang, Y.L. / Zhou, C.Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8wpz.cif.gz | 756.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8wpz.ent.gz | 635.3 KB | Display | PDB format |
PDBx/mmJSON format | 8wpz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wp/8wpz ftp://data.pdbj.org/pub/pdb/validation_reports/wp/8wpz | HTTPS FTP |
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-Related structure data
Related structure data | 37727MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 13349.196 Da / Num. of mol.: 8 / Source method: isolated from a natural source Source: (natural) Synechococcus elongatus PCC 7942 = FACHB-805 (bacteria) References: UniProt: Q31NB2 #2: Protein | Mass: 52516.605 Da / Num. of mol.: 8 / Source method: isolated from a natural source Source: (natural) Synechococcus elongatus PCC 7942 = FACHB-805 (bacteria) References: UniProt: Q31NB3, ribulose-bisphosphate carboxylase |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: subtomogram averaging |
-Sample preparation
Component | Name: RuBisCO / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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Source (natural) | Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (bacteria) |
Details of virus | Empty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRION |
Natural host | Organism: Nostoc sp. PCC 7120 = FACHB-418 |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 300 K |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 3.5 e/Å2 / Avg electron dose per subtomogram: 145 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
EM software | Name: RELION / Version: 3.1 / Category: 3D reconstruction | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 2700 / Symmetry type: POINT | ||||||||||||||||||||||||
EM volume selection | Num. of tomograms: 88 / Num. of volumes extracted: 29000 | ||||||||||||||||||||||||
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