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- EMDB-51067: Beta carbonic anhydrase CsoSCA from the Halothiobacillus neapolit... -
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Open data
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Basic information
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Title | Beta carbonic anhydrase CsoSCA from the Halothiobacillus neapolitanus alpha-carboxysome | |||||||||
![]() | Primary map | |||||||||
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![]() | Carbonic anhydrase / Carboxysome / rubisco / LYASE | |||||||||
Function / homology | ![]() carboxysome / carbon fixation / IgG binding / carbonic anhydrase / carbonate dehydratase activity / extracellular region / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.51 Å | |||||||||
![]() | Ng PC / Marles-Wright J / Basle A / Liu L | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Beta carbonic anhydrase CsoSCA from the Halothiobacillus neapolitanus alpha-carboxysome Authors: Ng PC / Marles-Wright J / Basle A / Liu L | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 32.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 23.2 KB 23.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.4 KB | Display | ![]() |
Images | ![]() | 74.8 KB | ||
Masks | ![]() | 64 MB | ![]() | |
Filedesc metadata | ![]() | 6.7 KB | ||
Others | ![]() ![]() ![]() | 59.7 MB 59.3 MB 59.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 832.5 KB | Display | ![]() |
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Full document | ![]() | 832.1 KB | Display | |
Data in XML | ![]() | 16.4 KB | Display | |
Data in CIF | ![]() | 21.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9g4tMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | Primary map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.0762 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Additional map: Sharpened map
File | emd_51067_additional_1.map | ||||||||||||
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Annotation | Sharpened map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map B
File | emd_51067_half_map_1.map | ||||||||||||
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Annotation | Half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map A
File | emd_51067_half_map_2.map | ||||||||||||
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Annotation | Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Carbonic anhydrase complex
Entire | Name: Carbonic anhydrase complex |
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Components |
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-Supramolecule #1: Carbonic anhydrase complex
Supramolecule | Name: Carbonic anhydrase complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 409 KDa |
-Macromolecule #1: Immunoglobulin G-binding protein G,Carboxysome shell carbonic anh...
Macromolecule | Name: Immunoglobulin G-binding protein G,Carboxysome shell carbonic anhydrase type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: carbonic anhydrase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 68.294305 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MWSHPQFEKG GGSGGGSGGS SAWSHPQFEK YKLILNGKTL KGETTTEAVD AATAEKVFKQ YANDNGVDGE WTYDDATKTF TVTEPMSDY DIPTTENLYF QGNTRNTRSK QRAPFGVSSS VKPRLDLIEQ APNPAYDRHP ACITLPERTC RHPLTDLEAN E QLGRCEDS ...String: MWSHPQFEKG GGSGGGSGGS SAWSHPQFEK YKLILNGKTL KGETTTEAVD AATAEKVFKQ YANDNGVDGE WTYDDATKTF TVTEPMSDY DIPTTENLYF QGNTRNTRSK QRAPFGVSSS VKPRLDLIEQ APNPAYDRHP ACITLPERTC RHPLTDLEAN E QLGRCEDS VKNRFDRVIP FLQVVAGIPL GLDYVTRVQE LAQSSLGHTL PEELLKDNWI SGHNLKGIFG YATAKALTAA TE QFSRKIM SEKDDSASAI GFFLDCGFHA VDISPCADGR LKGLLPYILR LPLTAFTYRK AYAGSMFDIE DDLAQWEKNE LRR YREGVP NTADQPTRYL KIAVYHFSTS DPTHSGCAAH GSNDRAALEA ALTQLMKFRE AVENAHCCGA SIDILLIGVD TDTD AIRVH IPDSKGFLNP YRYVDNTVTY AQTLHLAPDE ARVIIHEAIL NANRSDGWAK GNGVASEGMR RFIGQLLINN LSQID YVVN RHGGRYPPND IGHAERYISV GDGFDEVQIR NLAYYAHLDT VEENAIDVDV GIKIFTKLNL SRGLPIPIAI HYRYDP NVP GSRERTVVKA RRIYNAIKER FSSLDEQNLL QFRLSVQAQD IGSPIEEVAS A UniProtKB: Immunoglobulin G-binding protein G, Carboxysome shell carbonic anhydrase |
-Macromolecule #2: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 2 / Number of copies: 1 / Formula: ZN |
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Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1.5 mg/mL | ||||||||||||
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Buffer | pH: 8 Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 120 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.026000000000000002 kPa | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 240000 |
Sample stage | Cooling holder cryogen: NITROGEN |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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Details | Model fitting using ChimeraX |
Refinement | Space: REAL / Protocol: RIGID BODY FIT / Target criteria: Cross-correlation coefficient |
Output model | ![]() PDB-9g4t: |