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- EMDB-41432: C. elegans TMC-2 complex, focused refinement of dimer interface -
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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | C. elegans TMC-2 complex, focused refinement of dimer interface | |||||||||
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![]() | Mechanosensory transduction Macromolecular complex C. elegans / MEMBRANE PROTEIN | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Clark S / Jeong H / Goehring A / Posert R / Gouaux E | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Architecture of the TMC-2 complex from C. elegans Authors: Clark S / Jeong H / Goehring A / Posert R / Gouaux E | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 170.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.3 KB 15.3 KB | Display Display | ![]() |
Images | ![]() | 140.7 KB | ||
Filedesc metadata | ![]() | 5.4 KB | ||
Others | ![]() ![]() | 320.6 MB 320.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 870.3 KB | Display | ![]() |
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Full document | ![]() | 869.9 KB | Display | |
Data in XML | ![]() | 17.3 KB | Display | |
Data in CIF | ![]() | 20.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.831 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_41432_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_41432_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : C. elegans TMC-2 complex
Entire | Name: C. elegans TMC-2 complex |
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Components |
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-Supramolecule #1: C. elegans TMC-2 complex
Supramolecule | Name: C. elegans TMC-2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Transmembrane channel-like protein TMC-2
Macromolecule | Name: Transmembrane channel-like protein TMC-2 / type: protein_or_peptide / ID: 1 / Enantiomer: DEXTRO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MPKSGAHQPL VRHDTDDGGE TGQSVKSLAD VSEEEIDSRM SRRSSVIADL LSLFRRSSSV LVRPHTRLGN PNFDDDDDEF DEEDDKEASK DRILKKIQQK KEIIQKLRGQ PWYMKRKRRT LKVAQKHLQQ QEAKVSKARL YKAEAGRRLT QASRWLDNLK IYLIPWEAKI ...String: MPKSGAHQPL VRHDTDDGGE TGQSVKSLAD VSEEEIDSRM SRRSSVIADL LSLFRRSSSV LVRPHTRLGN PNFDDDDDEF DEEDDKEASK DRILKKIQQK KEIIQKLRGQ PWYMKRKRRT LKVAQKHLQQ QEAKVSKARL YKAEAGRRLT QASRWLDNLK IYLIPWEAKI RKIESHFGSV VSSYFTFHRW VLGVNITITF IMCMFVVIPE WLADSRTQFG DDRYNKTKAI KVMPPAVRAR ADELSTVWDF GGYFQYSLLF YGFYSKETFF GETIKYRVPV AYFFCNIFIL GFSLFIILRK MAANNRRGTL SSGKTQQYLF NWKAFTGWDY TIGNPETAGN VYMANVIKFR EAINDDKQKP SDKHPWIRFV ARVLTNLFIC AMYVFSIWAI MQCGTLKGEH FFAQNATAIT ISLITLVFPN IFDLLGKIEK LHPRNALRFQ LGRVLVLYIL NYYTLIYSLM LQLEHLQKEK NASDNPISAL GHPGDAIGRT IRETVLPRYP VDNNPHTYYS YAPVTTTPIP ATSSWTTVLP DFGPFGVYNP KASVTKDDTV FSSPVVETHM FGPNSDWNET TVNAASPTGA TTRASLRMSQ GGLCWETIIG QEITKLVTMD LYMTVASIFL IDFLRGLACR YLNLYWPWDL ERTFPEYGEF KVAENVLHLV NNQGMIWLGL FFVPLLPMLN NIKLIILMYI RGWAAMTCNV PASQIFRASR SSNFFFALLI LFLFLCTLPV GFVIASKTPS KSCGPFGNQS FFYSVITDVL HENLDKTLVN GIKYSLSPGI IIPVLVLLSL VIYFLIAMVT GLSQANQDLS FQLMVERTEE KKKIFELAGG KKKKSKDNTF GKQKPKQLLP PPTKGVSSDD DSQHNRSTAK SVSGRQFVPS LGSVSEVDHS TGEEQSSDSE STTSSLPPKL SLRQRFLVCI GWADPNKYGR HDDIEMEEGG GRLRELSTGS ETDSDDEDSE KSNRDMSYRT AIQSFDQNSQ SASASSSKST TTAPSNSEMR IEITENPLHT YITPLRIEKK SSASSSSSSH QPSSSIEKQA ARRLLQPIST THNIRYGVAT VENSSQDPTR PPSTDDSLGD PALHEPLWAN LNPHSSYTSA MMSPIMNEVM SNDETTDDEK GRLIPDRPPI PHSPRELKRL KREKDQQSES GSKPSTPRPP RFRISMSPPR KPPSEKNDSD SSNRKYEMRV EKSPKKPKKS DND |
-Macromolecule #2: Calcium and integrin binding protein CALM-1
Macromolecule | Name: Calcium and integrin binding protein CALM-1 / type: protein_or_peptide / ID: 2 / Enantiomer: DEXTRO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MGNNASSLSE LNLFSKGGVF TREQLDEYQD CTFFTRKDII RLYKRFYALN PHKVPTNMQG NRPAITTLTF EEVEKMPELK ENPFKRRICE VFSEDGRGNL SFDDFLDMFS VFSEMAPLQL KLKYAFRIYD YDGDELLGHD DLSKMIRSLT RDELSDVEVE FIIERIIEEA ...String: MGNNASSLSE LNLFSKGGVF TREQLDEYQD CTFFTRKDII RLYKRFYALN PHKVPTNMQG NRPAITTLTF EEVEKMPELK ENPFKRRICE VFSEDGRGNL SFDDFLDMFS VFSEMAPLQL KLKYAFRIYD YDGDELLGHD DLSKMIRSLT RDELSDVEVE FIIERIIEEA DLDGDSSINF AEFEHVVSRS PDFIRTFHIR I |
-Macromolecule #3: Transmembrane inner ear protein TMIE
Macromolecule | Name: Transmembrane inner ear protein TMIE / type: protein_or_peptide / ID: 3 / Enantiomer: DEXTRO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MPSGNEEINH LSALDQFVAP GLRLWMLIAL VGGVLLIMIV IVCCFMRIRI PRTKRQIDLI AAKRKLRKST KNSAEANAHN DERAQAIVMN SMPSGGGGGA PSTSSSRHTG SRIQSQV |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | tissue |
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Sample preparation
Concentration | 0.003 mg/mL |
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Buffer | pH: 8 / Details: 50 mM Tris pH 8.0, 150 mM NaCl, 0.02% GDN |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK IV |
Details | Native TMC-2 complex, isolated from transgenic C. elegans. |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 207726 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC |