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Yorodumi- PDB-5xti: Cryo-EM architecture of human respiratory chain megacomplex-I2III2IV2 -
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-Basic information
Entry | Database: PDB / ID: 5xti | ||||||||||||||||||
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Title | Cryo-EM architecture of human respiratory chain megacomplex-I2III2IV2 | ||||||||||||||||||
Components |
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Keywords | OXIDOREDUCTASE/ELECTRON TRANSPORT / Homo sapiens / Oxidoreductase / Respiratory / OXIDOREDUCTASE-ELECTRON TRANSPORT complex | ||||||||||||||||||
Function / homology | Function and homology information subthalamus development / pons development / positive regulation of peptidase activity / cerebellar Purkinje cell layer development / protein insertion into mitochondrial inner membrane / Complex I biogenesis / blastocyst hatching / pyramidal neuron development / ubiquinone-6 biosynthetic process / response to mercury ion ...subthalamus development / pons development / positive regulation of peptidase activity / cerebellar Purkinje cell layer development / protein insertion into mitochondrial inner membrane / Complex I biogenesis / blastocyst hatching / pyramidal neuron development / ubiquinone-6 biosynthetic process / response to mercury ion / TP53 Regulates Metabolic Genes / respiratory chain complex IV assembly / protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / thalamus development / mitochondrial respirasome assembly / Cytoprotection by HMOX1 / cellular response to oxygen levels / respiratory chain complex IV / Respiratory electron transport / iron-sulfur cluster assembly complex / mitochondrial respiratory chain complex III assembly / mitochondrial large ribosomal subunit binding / respiratory gaseous exchange by respiratory system / Mitochondrial protein import / regulation of oxidative phosphorylation / Respiratory electron transport / gliogenesis / mitochondrial respiratory chain complex III / neural precursor cell proliferation / mitochondrial respiratory chain complex IV / [2Fe-2S] cluster assembly / mitochondrial respirasome / cardiac muscle tissue development / NADH dehydrogenase activity / Glyoxylate metabolism and glycine degradation / response to alkaloid / oxygen sensor activity / cellular respiration / cytochrome-c oxidase / quinol-cytochrome-c reductase / ubiquinone binding / ubiquinol-cytochrome-c reductase activity / oxidative phosphorylation / acyl binding / response to copper ion / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / response to glucagon / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial ribosome / electron transport coupled proton transport / iron-sulfur cluster assembly / mitochondrial ATP synthesis coupled electron transport / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / acyl carrier activity / azurophil granule membrane / mitochondrial translation / hypothalamus development / midbrain development / NADH:ubiquinone reductase (H+-translocating) / sodium ion transport / response to cobalamin / proton motive force-driven mitochondrial ATP synthesis / mitochondrial respiratory chain complex I / apoptotic mitochondrial changes / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / RHOG GTPase cycle / NADH dehydrogenase (ubiquinone) activity / quinone binding / response to hyperoxia / ATP synthesis coupled electron transport / cellular response to interferon-beta / animal organ regeneration / negative regulation of intrinsic apoptotic signaling pathway / enzyme regulator activity / response to cadmium ion / respirasome / aerobic respiration / ATP metabolic process / cellular response to retinoic acid / extrinsic apoptotic signaling pathway / response to cAMP / response to organonitrogen compound / ionotropic glutamate receptor binding / substantia nigra development / reactive oxygen species metabolic process / cerebellum development / respiratory electron transport chain / neurogenesis / response to activity / regulation of mitochondrial membrane potential / response to nicotine / synaptic membrane / generation of precursor metabolites and energy / central nervous system development / fatty acid binding / apoptotic signaling pathway Similarity search - Function | ||||||||||||||||||
Biological species | Homo sapiens (human) Bos taurus (cattle) | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 17.4 Å | ||||||||||||||||||
Authors | Gu, J. / Wu, M. / Yang, M. | ||||||||||||||||||
Funding support | China, 5items
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Citation | Journal: Cell / Year: 2017 Title: Architecture of Human Mitochondrial Respiratory Megacomplex IIIIIV. Authors: Runyu Guo / Shuai Zong / Meng Wu / Jinke Gu / Maojun Yang / Abstract: The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, ...The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, we examined the human respiratory chain megacomplex-IIIIIV (MCIIIIIV) with 140 subunits and a subset of associated cofactors using cryo-electron microscopy. The MCIIIIIV forms a circular structure with the dimeric CIII located in the center, where it is surrounded by two copies each of CI and CIV. Two cytochrome c (Cyt.c) molecules are positioned to accept electrons on the surface of the c state CIII dimer. Analyses indicate that CII could insert into the gaps between CI and CIV to form a closed ring, which we termed the electron transport chain supercomplex. The structure not only reveals the precise assignment of individual subunits of human CI and CIII, but also enables future in-depth analysis of the electron transport chain as a whole. | ||||||||||||||||||
History |
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-Structure visualization
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Structure viewer | Molecule: MolmilJmol/JSmol |
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PDBx/mmCIF format | 5xti.cif.gz | 4.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb5xti.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 5xti.json.gz | Tree view | PDBx/mmJSON format | |
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-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xt/5xti ftp://data.pdbj.org/pub/pdb/validation_reports/xt/5xti | HTTPS FTP |
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-Related structure data
Related structure data | 6776MC 6771C 6772C 6773C 6774C 6775C 5xtbC 5xtcC 5xtdC 5xteC 5xthC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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-Components
-NADH dehydrogenase [ubiquinone] flavoprotein ... , 3 types, 6 molecules ABAKBKOBO
#1: Protein | Mass: 47323.938 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 27-457 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: P49821, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase #10: Protein/peptide | Mass: 3900.312 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 74-106 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P56181 #14: Protein | Mass: 23430.881 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 36-247 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: P19404, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase |
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-NADH dehydrogenase [ubiquinone] iron-sulfur protein ... , 7 types, 14 molecules BBBCBCLBLPBPQBQTBThBh
#2: Protein | Mass: 20314.037 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: O00217, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase #3: Protein | Mass: 17887.928 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 58-213 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: O75251, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase #11: Protein | Mass: 13721.598 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 58-175 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43181 #15: Protein | Mass: 24432.656 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 43-250 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: O75489, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase #16: Protein | Mass: 49236.480 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: O75306, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase #18: Protein | Mass: 10578.848 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 29-123 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75380 #31: Protein | Mass: 12314.254 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 2-105 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43920 |
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-NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 12 types, 24 molecules EBEFBFHBHIBIJBJNBNSBSUBUVBVWBWuBuwBw
#4: Protein | Mass: 13758.070 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 42-154 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P56556 #5: Protein | Mass: 9535.905 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 14-96 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43678 #7: Protein | Mass: 13119.208 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 5-116 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16718 #8: Protein | Mass: 12282.051 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 4-113 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95182 #9: Protein | Mass: 38387.594 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 40-376 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16795 #13: Protein | Mass: 16880.068 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 2-144 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UI09 #17: Protein | Mass: 8084.391 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O15239 #19: Protein | Mass: 9156.602 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95167 #20: Protein | Mass: 14736.853 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q86Y39 #21: Protein | Mass: 16132.570 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 7-144 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9P0J0 #42: Protein | Mass: 19853.736 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 4-172 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P51970 #44: Protein | Mass: 37200.270 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95299 |
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-Protein , 4 types, 10 molecules GXBGBXMBMAHAUAJAV
#6: Protein | Mass: 9845.247 Da / Num. of mol.: 4 / Fragment: UNP RESIDUES 72-196 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O14561 #12: Protein | Mass: 75471.484 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 30-716 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: P28331, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase #65: Protein | Mass: 27388.395 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P08574 #66: Protein | Mass: 42543.016 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 2-479 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P00156 |
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-NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 11 types, 22 molecules YBYZBZaBabBbcBcdBdeBenBnoBopBpvBv
#22: Protein | Mass: 7468.270 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 39-97 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95178 #23: Protein | Mass: 9261.605 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 10-89 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43676 #24: Protein | Mass: 16573.160 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 52-189 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43674 #25: Protein | Mass: 15008.635 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 3-126 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95139 #26: Protein | Mass: 18267.562 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 34-186 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95169 #27: Protein | Mass: 20721.650 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 1-171 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O96000 #28: Protein | Mass: 11494.942 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 54-150 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NX14 #37: Protein | Mass: 6741.883 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 3-58 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75438 #38: Protein | Mass: 15100.399 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95168 #39: Protein | Mass: 21189.141 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 8-179 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y6M9 #43: Protein | Mass: 14997.401 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 3-124 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P17568 |
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-NADH dehydrogenase [ubiquinone] 1 subunit ... , 2 types, 4 molecules fBfgBg
#29: Protein/peptide | Mass: 5704.602 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 28-74 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43677 #30: Protein | Mass: 14209.521 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95298 |
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-NADH-ubiquinone oxidoreductase chain ... , 7 types, 14 molecules iBijBjkBklBlmBmrBrsBs
#32: Protein | Mass: 39007.656 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: Q4GRX1, UniProt: P03891*PLUS, NADH:ubiquinone reductase (H+-translocating) #33: Protein | Mass: 13147.871 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 1-115 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: B9EE38, NADH:ubiquinone reductase (H+-translocating) #34: Protein | Mass: 10702.086 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 1-97 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: V9JN72, NADH:ubiquinone reductase (H+-translocating) #35: Protein | Mass: 67096.023 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: X5BVZ3, UniProt: P03915*PLUS, NADH:ubiquinone reductase (H+-translocating) #36: Protein | Mass: 18660.979 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: Q8HAX7, NADH:ubiquinone reductase (H+-translocating) #40: Protein | Mass: 51689.688 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: B2XJG5, UniProt: P03905*PLUS, NADH:ubiquinone reductase (H+-translocating) #41: Protein | Mass: 35621.215 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) References: UniProt: H9PGF0, NADH:ubiquinone reductase (H+-translocating) |
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-Cytochrome c oxidase subunit ... , 13 types, 26 molecules xBxyByzBz0B01B12B23B34B45B56B67B78B89B9
#45: Protein | Mass: 57065.844 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00396, cytochrome-c oxidase #46: Protein | Mass: 26040.393 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P68530 #47: Protein | Mass: 29957.627 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00415 #48: Protein | Mass: 16913.367 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 26-169 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00423 #49: Protein | Mass: 12453.081 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00426 #50: Protein | Mass: 10684.038 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00428 #51: Protein | Mass: 9452.687 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 13-96 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P07471 #52: Protein | Mass: 8925.979 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 12-86 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00429 #53: Protein | Mass: 8494.982 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P04038 #54: Protein | Mass: 6286.220 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 22-77 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P07470 #55: Protein/peptide | Mass: 5442.168 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 30-78 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P13183 #56: Protein/peptide | Mass: 5449.396 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00430 #57: Protein/peptide | Mass: 4738.523 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 25-67 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P10175 |
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-Cytochrome b-c1 complex subunit ... , 9 types, 18 molecules AAANABAOACAPADAQAEARAFASAGATAKAWALAY
#58: Protein | Mass: 9791.181 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O14949 #59: Protein | Mass: 5893.814 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 1-57 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P47985, quinol-cytochrome-c reductase #60: Protein | Mass: 21645.578 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P47985, quinol-cytochrome-c reductase #61: Protein | Mass: 7189.299 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UDW1 #62: Protein | Mass: 8861.742 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 18-91 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P07919 #63: Protein | Mass: 13037.842 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 6-111 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P14927 #64: Protein | Mass: 5958.912 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 2-52 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O14957 #67: Protein | Mass: 44946.582 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 35-453 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P22695 #68: Protein | Mass: 49181.430 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P31930 |
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-Non-polymers , 14 types, 100 molecules
#69: Chemical | ChemComp-SF4 / #70: Chemical | #71: Chemical | ChemComp-PLX / ( #72: Chemical | ChemComp-8Q1 / #73: Chemical | #74: Chemical | ChemComp-FES / #75: Chemical | ChemComp-CDL / #76: Chemical | ChemComp-PEE / #77: Chemical | ChemComp-CU / #78: Chemical | #79: Chemical | ChemComp-HEA / #80: Chemical | #81: Chemical | #82: Chemical | ChemComp-HEM / |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Human respiratory chain megacomplex-I2III2IV2 / Type: COMPLEX / Entity ID: #1-#68 / Source: NATURAL |
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Source (natural) | Organism: Homo sapiens (human) |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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: OTHER |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy |
Image recording | Electron dose: 1.25 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) |
-Processing
EM software |
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CTF correction | Type: NONE | ||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 17.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 8600 / Symmetry type: POINT |