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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-22018 | |||||||||
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Title | Pig R615C RyR1 in complex with CaM, EGTA (class 1, open) | |||||||||
![]() | RyR1, FKBP12.6, CaM | |||||||||
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![]() | receptor / calcium / channel / complex / TRANSPORT PROTEIN-ISOMERASE-CALCIUM BINDING PROTEIN complex | |||||||||
Function / homology | ![]() positive regulation of sequestering of calcium ion / negative regulation of calcium-mediated signaling / negative regulation of insulin secretion involved in cellular response to glucose stimulus / neuronal action potential propagation / negative regulation of release of sequestered calcium ion into cytosol / insulin secretion involved in cellular response to glucose stimulus / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events ...positive regulation of sequestering of calcium ion / negative regulation of calcium-mediated signaling / negative regulation of insulin secretion involved in cellular response to glucose stimulus / neuronal action potential propagation / negative regulation of release of sequestered calcium ion into cytosol / insulin secretion involved in cellular response to glucose stimulus / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / response to redox state / positive regulation of ryanodine-sensitive calcium-release channel activity / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Loss of phosphorylation of MECP2 at T308 / 'de novo' protein folding / CREB1 phosphorylation through the activation of Adenylate Cyclase / CaMK IV-mediated phosphorylation of CREB / PKA activation / negative regulation of high voltage-gated calcium channel activity / negative regulation of heart rate / Glycogen breakdown (glycogenolysis) / CLEC7A (Dectin-1) induces NFAT activation / Activation of RAC1 downstream of NMDARs / organelle localization by membrane tethering / negative regulation of ryanodine-sensitive calcium-release channel activity / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / FK506 binding / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / presynaptic endocytosis / Synthesis of IP3 and IP4 in the cytosol / regulation of cell communication by electrical coupling involved in cardiac conduction / Phase 0 - rapid depolarisation / calcineurin-mediated signaling / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / RHO GTPases activate PAKs / Ion transport by P-type ATPases / Uptake and function of anthrax toxins / regulation of ryanodine-sensitive calcium-release channel activity / Long-term potentiation / protein phosphatase activator activity / Calcineurin activates NFAT / Regulation of MECP2 expression and activity / smooth muscle contraction / DARPP-32 events / catalytic complex / Smooth Muscle Contraction / detection of calcium ion / regulation of cardiac muscle contraction / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / T cell proliferation / calcium channel inhibitor activity / cellular response to interferon-beta / Protein methylation / presynaptic cytosol / Activation of AMPK downstream of NMDARs / Ion homeostasis / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / eNOS activation / titin binding / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / sperm midpiece / voltage-gated potassium channel complex / regulation of calcium-mediated signaling / release of sequestered calcium ion into cytosol / calcium channel complex / substantia nigra development / FCERI mediated Ca+2 mobilization / sarcoplasmic reticulum membrane / calcium channel regulator activity / Ras activation upon Ca2+ influx through NMDA receptor / regulation of heart rate / FCGR3A-mediated IL10 synthesis / calyx of Held / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / protein maturation / adenylate cyclase activator activity / sarcomere / VEGFR2 mediated cell proliferation / regulation of cytokinesis / protein serine/threonine kinase activator activity / VEGFR2 mediated vascular permeability / spindle microtubule / peptidyl-prolyl cis-trans isomerase activity / Translocation of SLC2A4 (GLUT4) to the plasma membrane / peptidylprolyl isomerase / positive regulation of receptor signaling pathway via JAK-STAT / RAF activation / calcium-mediated signaling / Transcriptional activation of mitochondrial biogenesis / cellular response to type II interferon / Stimuli-sensing channels / long-term synaptic potentiation / Z disc / response to calcium ion Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||
![]() | Woll KW / Haji-Ghassemi O | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM. Authors: Kellie A Woll / Omid Haji-Ghassemi / Filip Van Petegem / ![]() Abstract: Ryanodine Receptors (RyRs) are massive channels that release Ca from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to malignant hyperthermia (MH), myopathies, and ...Ryanodine Receptors (RyRs) are massive channels that release Ca from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to malignant hyperthermia (MH), myopathies, and arrhythmias. Here, we explore the first MH mutation identified in humans by providing cryo-EM snapshots of the pig homolog, R615C, showing that it affects an interface between three solenoid regions. We also show the impact of apo-calmodulin (apoCaM) and how it can induce opening by bending of the bridging solenoid, mediated by its N-terminal lobe. For R615C RyR1, apoCaM binding abolishes a pathological 'intermediate' conformation, distributing the population to a mixture of open and closed channels, both different from the structure without apoCaM. Comparisons show that the mutation primarily affects the closed state, inducing partial movements linked to channel activation. This shows that disease mutations can cause distinct pathological conformations of the RyR and facilitate channel opening by disrupting interactions between different solenoid regions. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 54.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.6 KB 18.6 KB | Display Display | ![]() |
Images | ![]() | 214.5 KB | ||
Filedesc metadata | ![]() | 7.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 454 KB | Display | ![]() |
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Full document | ![]() | 453.5 KB | Display | |
Data in XML | ![]() | 7.7 KB | Display | |
Data in CIF | ![]() | 8.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6x35MC ![]() 6w1nC ![]() 6x32C ![]() 6x33C ![]() 6x34C ![]() 6x36C C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | RyR1, FKBP12.6, CaM | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.09 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : ryanodine receptor-FKBP1B-calmodulin complex
Entire | Name: ryanodine receptor-FKBP1B-calmodulin complex |
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Components |
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-Supramolecule #1: ryanodine receptor-FKBP1B-calmodulin complex
Supramolecule | Name: ryanodine receptor-FKBP1B-calmodulin complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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-Supramolecule #2: ryanodine receptor
Supramolecule | Name: ryanodine receptor / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2 |
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Source (natural) | Organism: ![]() ![]() |
-Supramolecule #3: FKBP1B
Supramolecule | Name: FKBP1B / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
-Supramolecule #4: Calmodulin
Supramolecule | Name: Calmodulin / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Peptidyl-prolyl cis-trans isomerase FKBP1B
Macromolecule | Name: Peptidyl-prolyl cis-trans isomerase FKBP1B / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 11.939562 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: SNAGVEIETI SPGDGRTFPK KGQTCVVHYT GMLQNGKKFD SSRDRNKPFK FRIGKQEVIK GFEEGAAQMS LGQRAKLTCT PDVAYGATG HPGVIPPNAT LIFDVELLNL E UniProtKB: Peptidyl-prolyl cis-trans isomerase FKBP1B |
-Macromolecule #2: Ryanodine Receptor
Macromolecule | Name: Ryanodine Receptor / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 423.654469 KDa |
Sequence | String: QFLRTDDEVV LQCNATVLKE QLKLCLAAEG FGNRLCFLEP TSNAQNVPPD LAICCFVLEQ SLSVRALQEM LANGHRTLLY GHAILLRHA HSGMYLSCLT TSRSMTDKLA FDVGLQEDAT GEACWWTTHP ASKQRSEGEK VRVGDDLILV SVSSERYLHL S TASGELQV ...String: QFLRTDDEVV LQCNATVLKE QLKLCLAAEG FGNRLCFLEP TSNAQNVPPD LAICCFVLEQ SLSVRALQEM LANGHRTLLY GHAILLRHA HSGMYLSCLT TSRSMTDKLA FDVGLQEDAT GEACWWTTHP ASKQRSEGEK VRVGDDLILV SVSSERYLHL S TASGELQV DASFMQTLWN MNPICSGCEE GYVTGGHVLR LFHGHMDECL TISPADQRRL VYYEGGSVCT HARSLWRLEP LR ISWSGSH LRWGQPLRIR HVTTGRYLAL IEDQGLVVVD ASKAHTKATS FCFRISKEKL KRDVEGMGPP EIKYGESLCF VQH VASGLW LTYAALKKKA ILHQEGHMDD ALSLTRCQQE ESQAARMIYS TAGLYNHFIK GLDSFSGKPR PAGTALPLEG VILS LQDLI GYFEPPSEEL QHEEKQSKLR SLRNRQSLFQ EEGMLSLVLN CIDRLNVYTT AAHFAEFAGE EAAESWKEIV NLLYE ILAS LIRGNRANCA LFSNNLDWLV SKLDRLEASS GILEVLYCVL IESPEVLNII QENHIKSIIS LLDKHGRNHK VLDVLC SLC VCNGVAVCSN QDLITENLLP GRELLLQTNL INYVTSIRPN IFVGRAEGTT QYSKWYFEVM VDEVVPFLTA QATHLRV GW ALTEGYSPYP GGGEGWGGNG VGDDLYSYGF DGLHLWTGHV PRLVTSPGQH LLAPEDVVSC CLDLSVPSIS FRINGCPV Q GVFEAFNLNG LFFPVVSFSA GVKVRFLLGG RHGEFKFLPP PGYAPCHEAV LPRERLRLEP IKEYRREGPR GPHLVGPSR CLSHTDFVPC PLPPHLERIR EKLAENIHEL WALTRIEQGW TYGPVRDDNK RLHPCLVDFH SLPEPERNYN LQMSGETLKT LLALGCHVG MADEKAEDNL RKTKLPKTYM MSNGYKPAPL DLSHVRLTPA QTTLVDRLAE NGHNVWARDR VAQGWSYSAV Q DIPARRNP RLVPYRLLDE ATKRSNRDSL CQAVRTLLGY GRVRIFRAEK SYAVQSGRWY FEFEAVTTGE MRVGWARPEL RP DVELGAD ELAYVFNGHR GQRWHLGSEL FGRPWQSGDV VGCMIDLTEN TIIFTLNGEV LMSDSGSETA FRDIEVGDGF LPV CSLGPG QVGHLNLGQD VSSLRFFAIC GLQEGFEPFA INMQRPVTTW FSKSLPQFEA VPLEHPHYEV SRVDGTVDTP PCLR LTHRS LVEMLFLRLS LPVQFHQLNT TTYYYSVRVF AGQEPSCVWV GWVTPDYHQH DMNFDLTKVR AVTVTMGDNI HSSLK CSNC YMVWGGDFVS HTDLVIGCLV DLATGLMTFT ANGKESNTFF QVEPNTKLFP AVFVLPTHQN VIQFELGKQK NIMPLS AAM FLSERKNPAP QCPPRLEMQM LMPVSWSRMP NHFLRVETRR AGERLGWAVQ CQEPLTMMAL HIPEENRCMD ILELSER LD LQQFHSHTLR LYRAVCALGN NRVAHALCSH VDQAQLLHAL EDAHLPGPLR AGYYDLLISI HLESACRSRR SMLSEYIV P LTPETRAITL FPPRHGLPGV GVTTSLRPPH HFSAPCFVAA LPEAPARLSP SIPLEALRDK ALRMLGEAVR DGGQHARDP VGGSVEFQFV PVLKLVSTLL VMGIFGDEDV KQILKMIEPE VEEGLLQMKL PESVKLQMCN LLEYFCDQEL QHRVESLAAF AERYVDKLQ ANQRDRYGIL MKAFTMTAAE TARRTREFRS PPQEQINMLL HFKPLPDEIR QDLLEFHQDL LTHCGIQLQS L QELVSHTV VRWAQEDFVQ SPELVRAMFS LLHRQYDGLG ELLRALPRAY TISPSSVEDT MSLLECLGQI RSLLIVQMGP QE ENLMIQS IGNIMNNKVF YQHPNLMRAL GMHETVMEVM VNVLGRFPKM VTSCCRFLCY FCRISRQNQR SMFDHLSYLL ENS GSTPLD VAAASVIDNN ELALALQEQD LEKVVSYLAG CGLQSCPMLL AKGYPDIGWN PCGGERYLDF LRFAVFVNGE SVEE NANVV VRLLIRKPEC FGPALRLLAT IEEAIGHAIM SFYAALIDLL GRCAPEMHLI QAGKGEALRI RAILRSLVPL DDLVG IISL PLQIPLMSAS FVPDHKASMV LFLDRVYGIE FLLHVLDVGF EMALALNRYL CLAVLPLITK CAPLFAMVDS MLHTVY RLS RGRSLTKAQR DVIEECLMAL CRYIRPSMLQ HLLRRLVF(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)DPR PVETLNVIIP EKLDSFINKF AEYTHEKWAF DKIQNNWSYG EN IDEELKT HPMLRPYKTF SEKDKEIYRW PIKESLKAMI AWEWTIEKAR EGEYNPQPPD LSGVTLSREL QAMAEQLAEN YHN TWGRKK KQELEAKGGG THPLLVPYDT LTAKEKARDR EKAQELLKFL QMNGYAVTR(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)EFSVLCR DLYALYPLLI RYVDNNRAHW LTEPNPSAEE LFRMVGEI F IYWSKSHNFK REEQNFVV(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) RRAVVACFRM TPLYNLPTHR ACNMFLESYK AAWILTEDHS FEDRMIDDL SKAGEQEEEE EEVEEKKPDP LHQLVLHFSR TALTEKSKLD EDYLYMAYAD IMAKSCHLEE SFEEKEMEKQ R LLYQQARL HNRGAAEMVL QMISACKGET GAMVSSTLKL GISILNGGNA DVQQKMLDYL KDKKEVGFFQ SIQALMQTCS VL DLNAFER QNKAEGLGMV NEDGTVIGEK VMADDEFTQD LFRFLQLLCE GHNNDFQNYL RTQTGNTTTI NIIICTVDYL LRL QESISD FYWYYSGKDV IEEQGKRNFS KAMSVAKQVF NSLTEYIQGP CTGNQQSLAH SRLWDAVVGF LHVFAHMMMK LAQD SSQIE LLKELLDLQK DMVVMLLSLL EGNVVNGMIA RQMVDMLVES SSNVEMILKF FDMFLKLKDI VGSEAFQDYV TDPRG LISK KDFQK(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)EEFANRFQE PARDIGFNVA VLLTNLSEHV PHDPRLRNFL EL AESILEY FRPYLGRIEI MGASRRIERI YFEISETNRA QWEMPQVKES KRQFIFDVVN EGGESEKMEL FVSFCEDTIF EMQ (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)EVQRVKFL NYLSRNFYTL RFLALFLAFA INFILLFYKV SDSPPVYYFL EESTGYMEPA LRCLSLLHTL VAFLCII GY NCLKVPLVIF KREKELARKL EFDGLYITEQ PEDDDVKGQW DRLVLNTPSF PSNYWDKFVK RKVLDKHGDI YGRERIAE G LLTWLMSIDV KYQIWKFGVI FTDNSFLYLG WYMVMSLLGH YNNFFFAAHL LDIAMGVKTL RTILSSVTHN GKQLVMTVG LLAVVVYLYT VVAFNFFRKF YNKSEDEDEP DMKCDDMMTC YLFHMYVGVR AGGGIGDEIE DPAGDEYELY RVVFDITFFF FVIVILLAI IQGLIIDAFG ELRDQQEQVR EDMETKCFIC GIGSDYFDTT PHRFETHTLE EHNLANYMFF LMYLINKDET E HTGQESYV WKMYQERCWD FFPAGDCFRK QYEDQL |
-Macromolecule #3: Calmodulin-1
Macromolecule | Name: Calmodulin-1 / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 16.723365 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREA FRVFDKDGNG YISAAELRHV MTNLGEKLTD EEVDEMIREA DIDGDGQVNY EEFVQMMTA UniProtKB: Calmodulin-1 |
-Macromolecule #4: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 4 / Number of copies: 4 / 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
Buffer | pH: 7.5 |
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Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: DIFFRACTION |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: PDB ENTRY |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: PHENIX (ver. dev-3714) / Number images used: 25122 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |