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- EMDB-70600: Cryo-EM Structure of Pig Ryanodine Receptor 1 R615C Mutant: Drug ... -

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Basic information

Entry
Database: EMDB / ID: EMD-70600
TitleCryo-EM Structure of Pig Ryanodine Receptor 1 R615C Mutant: Drug Bound Closed Conformation Consensus Map
Map dataConsensus Map
Sample
  • Organelle or cellular component: Ryanodine Receptor 1 and FKBP12.6 complex
    • Protein or peptide: pig Ryanodine Receptor 1 R615C mutant
    • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B
KeywordsIon Channel / Calcium Channel / TRANSPORT PROTEIN
Function / homology
Function and homology information


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 / terminal cisterna / ryanodine-sensitive calcium-release channel activity / ryanodine receptor complex / release of sequestered calcium ion into cytosol by sarcoplasmic reticulum ...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 / terminal cisterna / ryanodine-sensitive calcium-release channel activity / ryanodine receptor complex / release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / response to redox state / ossification involved in bone maturation / negative regulation of heart rate / cellular response to caffeine / 'de novo' protein folding / skin development / FK506 binding / organelle membrane / smooth endoplasmic reticulum / outflow tract morphogenesis / smooth muscle contraction / T cell proliferation / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / voltage-gated calcium channel activity / calcium channel inhibitor activity / skeletal muscle fiber development / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / Ion homeostasis / release of sequestered calcium ion into cytosol / calcium channel complex / sarcoplasmic reticulum membrane / cellular response to calcium ion / muscle contraction / sarcoplasmic reticulum / protein maturation / calcium channel regulator activity / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / calcium-mediated signaling / sarcolemma / calcium ion transmembrane transport / Stimuli-sensing channels / calcium channel activity / Z disc / intracellular calcium ion homeostasis / positive regulation of cytosolic calcium ion concentration / protein refolding / protein homotetramerization / transmembrane transporter binding / calmodulin binding / signaling receptor binding / calcium ion binding / ATP binding / membrane / cytoplasm
Similarity search - Function
Ryanodine receptor, SPRY domain 2 / : / Ryanodine receptor junctional solenoid repeat / Ryanodine Receptor TM 4-6 / Ryanodine receptor / Ryanodine receptor, SPRY domain 1 / Ryanodine receptor, SPRY domain 3 / Ryanodine Receptor TM 4-6 / Ryanodine receptor Ryr / RyR domain ...Ryanodine receptor, SPRY domain 2 / : / Ryanodine receptor junctional solenoid repeat / Ryanodine Receptor TM 4-6 / Ryanodine receptor / Ryanodine receptor, SPRY domain 1 / Ryanodine receptor, SPRY domain 3 / Ryanodine Receptor TM 4-6 / Ryanodine receptor Ryr / RyR domain / RyR/IP3 receptor binding core, RIH domain superfamily / : / RyR/IP3R Homology associated domain / Inositol 1,4,5-trisphosphate/ryanodine receptor / RIH domain / RyR and IP3R Homology associated / Inositol 1,4,5-trisphosphate/ryanodine receptor / RIH domain / : / MIR motif / MIR domain / MIR domain profile. / Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases / Mir domain superfamily / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / SPRY domain / FKBP-type peptidyl-prolyl cis-trans isomerase / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / Peptidyl-prolyl cis-trans isomerase domain superfamily / Ion transport domain / Ion transport protein / EF-hand domain pair / Concanavalin A-like lectin/glucanase domain superfamily
Similarity search - Domain/homology
Ryanodine receptor 1 / Peptidyl-prolyl cis-trans isomerase FKBP1B
Similarity search - Component
Biological speciesSus scrofa (pig) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.08 Å
AuthorsMolinarolo SM / Van Petegem F
Funding support Canada, 1 items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR) Canada
CitationJournal: Nat Commun / Year: 2025
Title: Cryo-electron microscopy reveals sequential binding and activation of Ryanodine Receptors by statin triplets.
Authors: Steven Molinarolo / Carmen R Valdivia / Héctor H Valdivia / Filip Van Petegem /
Abstract: Statins are the most prescribed class of drugs and inhibit a key enzyme in the cholesterol biosynthesis pathway. Many patients have reported mild to severe muscle related symptoms and a subset are at ...Statins are the most prescribed class of drugs and inhibit a key enzyme in the cholesterol biosynthesis pathway. Many patients have reported mild to severe muscle related symptoms and a subset are at risk for rhabdomyolysis. Sequence variants in RyR1, the skeletal muscle Ryanodine Receptor, correlate with intolerance to statins, but whether RyR1 can bind statins directly has remained unclear. Here we report cryo-EM structures of RyR1 in the absence and presence of atorvastatin, firmly establishing RyR1 as an unintended off-target. Our results show an unusual binding mode whereby three atorvastatin molecules bind together in a cleft formed by the pseudo-voltage sensing domain, making extensive interactions with each other and with RyR1. Atorvastatin activates RyR1 in a sequential way, whereby one statin per subunit can bind to the transmembrane region of a closed RyR1, with small structural perturbations that prime the channel for opening. Binding of two additional statins per subunit is associated with a widening of the pseudo-voltage sensing domain that triggers opening of the pore. Comparison with atorvastatin binding to HMG-CoA reductase, its intended target, offers clues on how to modify the statin to reduce RyR1 binding, while leaving binding to HMG-CoA reductase unperturbed.
History
DepositionMay 12, 2025-
Header (metadata) releaseJan 21, 2026-
Map releaseJan 21, 2026-
UpdateJan 21, 2026-
Current statusJan 21, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_70600.png

Downloads & links

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Map

FileDownload / File: emd_70600.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationConsensus Map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.96 Å/pix.
x 512 pix.
= 491.52 Å		0.96 Å/pix.
x 512 pix.
= 491.52 Å		0.96 Å/pix.
x 512 pix.
= 491.52 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.96 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.032
Minimum - Maximum-0.026123745 - 0.090641916
Average (Standard dev.)0.00040930457 (±0.0052323975)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 491.52 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Consensus Half A

Fileemd_70600_half_map_1.map
AnnotationConsensus Half A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Consensus Half B

Fileemd_70600_half_map_2.map
AnnotationConsensus Half B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Ryanodine Receptor 1 and FKBP12.6 complex

EntireName: Ryanodine Receptor 1 and FKBP12.6 complex
Components
  • Organelle or cellular component: Ryanodine Receptor 1 and FKBP12.6 complex
    • Protein or peptide: pig Ryanodine Receptor 1 R615C mutant
    • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B

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Supramolecule #1: Ryanodine Receptor 1 and FKBP12.6 complex

SupramoleculeName: Ryanodine Receptor 1 and FKBP12.6 complex / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 2.39 MDa

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Macromolecule #1: pig Ryanodine Receptor 1 R615C mutant

MacromoleculeName: pig Ryanodine Receptor 1 R615C mutant / type: protein_or_peptide / ID: 1 / Details: Pig RyR1 with R615C / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
SequenceString: MGDGGEGEDE VQFLRTDDEV VLQCNATVLK EQLKLCLAAE GFGNRLCFLE PTSNAQNVPP DLAICCFVL EQSLSVRALQ EMLANTVEAG VESSQGGGHR TLLYGHAILL RHAHSGMYLS C LTTSRSMT DKLAFDVGLQ EDATGEACWW TTHPASKQRS EGEKVRVGDD ...String:
MGDGGEGEDE VQFLRTDDEV VLQCNATVLK EQLKLCLAAE GFGNRLCFLE PTSNAQNVPP DLAICCFVL EQSLSVRALQ EMLANTVEAG VESSQGGGHR TLLYGHAILL RHAHSGMYLS C LTTSRSMT DKLAFDVGLQ EDATGEACWW TTHPASKQRS EGEKVRVGDD LILVSVSSER YL HLSTASG ELQVDASFMQ TLWNMNPICS GCEEGYVTGG HVLRLFHGHM DECLTISPAD SDD QRRLVY YEGGSVCTHA RSLWRLEPLR ISWSGSHLRW GQPLRIRHVT TGRYLALIED QGLV VVDAS KAHTKATSFC FRISKEKLDT APKRDVEGMG PPEIKYGESL CFVQHVASGL WLTYA APDP KALRLGVLKK KAILHQEGHM DDALSLTRCQ QEESQAARMI YSTAGLYNHF IKGLDS FSG KPRGSGAPAG TALPLEGVIL SLQDLIGYFE PPSEELQHEE KQSKLRSLRN RQSLFQE EG MLSLVLNCID RLNVYTTAAH FAEFAGEEAA ESWKEIVNLL YEILASLIRG NRANCALF S NNLDWLVSKL DRLEASSGIL EVLYCVLIES PEVLNIIQEN HIKSIISLLD KHGRNHKVL DVLCSLCVCN GVAVCSNQDL ITENLLPGRE LLLQTNLINY VTSIRPNIFV GRAEGTTQYS KWYFEVMVD EVVPFLTAQA THLRVGWALT EGYSPYPGGG EGWGGNGVGD DLYSYGFDGL H LWTGHVPR LVTSPGQHLL APEDVVSCCL DLSVPSISFR INGCPVQGVF EAFNLNGLFF PV VSFSAGV KVRFLLGGRH GEFKFLPPPG YAPCHEAVLP RERLRLEPIK EYRREGPRGP HLV GPSRCL SHTDFVPCPV DTVQIVLPPH LERIREKLAE NIHELWALTR IEQGWTYGPV RDDN KRLHP CLVDFHSLPE PERNYNLQMS GETLKTLLAL GCHVGMADEK AEDNLRKTKL PKTYM MSNG YKPAPLDLSH VRLTPAQTTL VDRLAENGHN VWARDRVAQG WSYSAVQDIP ARRNPR LVP YRLLDEATKR SNRDSLCQAV RTLLGYGYNI EPPDQEPSQV ESQSRWDRVR IFRAEKS YA VQSGRWYFEF EAVTTGEMRV GWARPELRPD VELGADELAY VFNGHRGQRW HLGSELFG R PWQSGDVVGC MIDLTENTII FTLNGEVLMS DSGSETAFRD IEVGDGFLPV CSLGPGQVG HLNLGQDVSS LRFFAICGLQ EGFEPFAINM QRPVTTWFSK SLPQFEAVPL EHPHYEVSRV DGTVDTPPC LRLTHRTWGS QNSLVEMLFL RLSLPVQFHQ HFRCTAGATP LAPPGLQPPA E DEARAAEP DPDYENLRRS AGRWGEAEGG KEGTAKEGAP GGTAQAGVEA QPPRAENEKD AT TEKNKKR GFLFKAKKAA MMTQPPATPT LPRLPHEVVP ADDRDDPDII LNTTTYYYSV RVF AGQEPS CVWVGWVTPD YHQHDMNFDL TKVRAVTVTM GDEQGNIHSS LKCSNCYMVW GGDF VSPGQ QGRISHTDLV IGCLVDLATG LMTFTANGKE SNTFFQVEPN TKLFPAVFVL PTHQN VIQF ELGKQKNIMP LSAAMFLSER KNPAPQCPPR LEMQMLMPVS WSRMPNHFLR VETRRA GER LGWAVQCQEP LTMMALHIPE ENRCMDILEL SERLDLQQFH SHTLRLYRAV CALGNNR VA HALCSHVDQA QLLHALEDAH LPGPLRAGYY DLLISIHLES ACRSRRSMLS EYIVPLTP E TRAITLFPPG KRTENGPRRH GLPGVGVTTS LRPPHHFSAP CFVAALPAVG AAEAPARLS PSIPLEALRD KALRMLGEAV RDGGQHARDP VGGSVEFQFV PVLKLVSTLL VMGIFGDEDV KQILKMIEP EVFTEEEEEE EEEEEEEEED EEEKEEDEEE EAREKEDEEK EEEETAEGEK E EYLEEGLL QMKLPESVKL QMCNLLEYFC DQELQHRVES LAAFAERYVD KLQANQRDRY GI LMKAFTM TAAETARRTR EFRSPPQEQI NMLLHFKDGE DEEDCPLPDE IRQDLLEFHQ DLL THCGIQ LEGEEEEPEE EATLGSRLMS LLEKVRLVKK KEEKSEEEPP AEESKAQSLQ ELVS HTVVR WAQEDFVQSP ELVRAMFSLL HRQYDGLGEL LRALPRAYTI SPSSVEDTMS LLECL GQIR SLLIVQMGPQ EENLMIQSIG NIMNNKVFYQ HPNLMRALGM HETVMEVMVN VLGGGE SKE IRFPKMVTSC CRFLCYFCRI SRQNQRSMFD HLSYLLENSG IGLGMQGSTP LDVAAAS VI DNNELALALQ EQDLEKVVSY LAGCGLQSCP MLLAKGYPDI GWNPCGGERY LDFLRFAV F VNGESVEENA NVVVRLLIRK PECFGPALRG EGGSGLLATI EEAIRISEDP ARDGPGVRR DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE MHLIQAGKGE ALRIRAILRS LVPLDDLVG IISLPLQIPT LGKDGALVQP KMSASFVPDH KASMVLFLDR VYGIENQDFL L HVLDVGFL PDMRAAASLD TATFSTTEMA LALNRYLCLA VLPLITKCAP LFAGTEHRAI MV DSMLHTV YRLSRGRSLT KAQRDVIEEC LMALCRYIRP SMLQHLLRRL VFDVPILNEF AKM PLKLLT NHYERCWKYY CLPTGWANFG VTSEEELHLT RKLFWGIFDS LAHKKYDPEL YRMA MPCLC AIAGALPPDY VDASYSSKAE KKATVDAEGN FDPRPVETLN VIIPEKLDSF INKFA EYTH EKWAFDKIQN NWSYGENIDE ELKTHPMLRP YKTFSEKDKE IYRWPIKESL KAMIAW EWT IEKAREGEEE KTEKKKTRKI SQSAQTYDAR EGYNPQPPDL SGVTLSRELQ AMAEQLA EN YHNTWGRKKK QELEAKGGGT HPLLVPYDTL TAKEKARDRE KAQELLKFLQ MNGYAVTR G LKDMELDTSS IEKRFAFGFL QQLLRWMDIS QEFIAHLEAV VSSGRVEKSP HEQEIKFFA KILLPLINQY FTNHCLYFLS TPAKVLGSGG HASNKEKEMI TSLFCKLAAL VRHRVSLFGT DAPAVVNCL HILARSLDAR TVMKSGPEIV KAGLRSFFES ASEDIEKMVE NLRLGKVSQA R TQVKGVGQ NLTYTTVALL PVLTTLFQHI AQHQFGDDVI LDDVQVSCYR TLCSIYSLGT TR NPYVEKL RPALGECLAR LAAAMPVAFL EPQLNEYNAC SVYTTKSPRE RAILGLPNSV EEM CPDIPV LERLMADIGG LAESGARYTE MPHVIEITLP MLCSYLPRWW ERGPEAPPPA LPAG APPPC TAVTSDHLNS LLGNILRIIV NNLGIDEASW MKRLAVFAQP IVSRARPELL HSHFI PTIG RLRKRAGKVV AEEEQLRLEA KAEAEEGELL VRDEFSVLCR DLYALYPLLI RYVDNN RAH WLTEPNPSAE ELFRMVGEIF IYWSKSHNFK REEQNFVVQN EINNMSFLTA DNKSKMA KS GGSDQERTKK KRLGDRYSVQ TSLIVATLKK MLPIGLNMCA PTDQELITLA KTRYALKD T DEEVREFLQN NLHLQGKVEG SPSLRWQMAL YRGLPGREED ADDPEKIVRR VQEVSAVLY HLEQMEHPYK SKKAVWHKLL SKQRRRAVVA CFRMTPLYNL PTHRACNMFL ESYKAAWILT EDHSFEDRM IDDLSKAGEQ EEEEEEVEEK KPDPLHQLVL HFSRTALTEK SKLDEDYLYM A YADIMAKS CHLEEGGENG EAQEEVEVSF EEKEMEKQRL LYQQARLHNR GAAEMVLQMI SA CKGETGA MVSSTLKLGI SILNGGNADV QQKMLDYLKD KKEVGFFQSI QALMQTCSVL DLN AFERQN KAEGLGMVNE DGTVINRQNG EKVMADDEFT QDLFRFLQLL CEGHNNDFQN YLRT QTGNT TTINIIICTV DYLLRLQESI SDFYWYYSGK DVIEEQGKRN FSKAMSVAKQ VFNSL TEYI QGPCTGNQQS LAHSRLWDAV VGFLHVFAHM MMKLAQDSSQ IELLKELLDL QKDMVV MLL SLLEGNVVNG MIARQMVDML VESSSNVEMI LKFFDMFLKL KDIVGSEAFQ DYVTDPR GL ISKKDFQKAM DSQKQFTGPE IQFLLSCSEA DENEMIDCEE FANRFQEPAR DIGFNVAV L LTNLSEHVPH DPRLRNFLEL AESILEYFRP YLGRIEIMGA SRRIERIYFE ISETNRAQW EMPQVKESKR QFIFDVVNEG GESEKMELFV SFCEDTIFEM QIAAQISEPE GEPEEDEDEG AGLAEAGAE GAEEGAVGPE GAAGTAAAGL TARLAAATSR ALRGLSYRSL RRRVRRLRRL T AREAATAL AALLWAALAH AGAAGAGAAA GALRLLWGSL FGGGLVEGAK KVTVTELLAG MP DPTGDEV HGEQPAGPGG EADGEGAGEG AGEAWEGAGD EEVAVQEAGP GGADGAVAVA EGG PFRPEG AGGLGDMGDT TPAEPPTPEG SPIIKRKLGV DGEEEELPPE PEPEPEPEPE KADA ENGEK EEVPKPPPEP PKKTAPPPPP PKKEEGGSGG LEFWGELEVQ RVKFLNYLSR NFYTL RFLA LFLAFAINFI LLFYKVSDSP PGEDDMEGSA AGDLSGAGSG GGSGWGSGAG EEVEGD EDE NMVYYFLEES TGYMEPALRC LSLLHTLVAF LCIIGYNCLK VPLVIFKREK ELARKLE FD GLYITEQPED DDVKGQWDRL VLNTPSFPSN YWDKFVKRKV LDKHGDIYGR ERIAELLG M DLATLEITAH NERKPEPPPG LLTWLMSIDV KYQIWKFGVI FTDNSFLYLG WYMVMSLLG HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT VVAFNFFRKF YNKSEDEDE PDMKCDDMMT CYLFHMYVGV RAGGGIGDEI EDPAGDEYEL YRVVFDITFF F FVIVILLA IIQGLIIDAF GELRDQQEQV REDMETKCFI CGIGSDYFDT TPHRFETHTL EE HNLANYM FFLMYLINKD ETEHTGQESY VWKMYQERCW DFFPAGDCFR KQYEDQLS

UniProtKB: Ryanodine receptor 1

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Macromolecule #2: Peptidyl-prolyl cis-trans isomerase FKBP1B

MacromoleculeName: Peptidyl-prolyl cis-trans isomerase FKBP1B / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GVEIETISPG DGRTFPKKGQ TCVVHYTGML QNGKKFDSSR DRNKPFKFRI GKQEVIKGF EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF DVELLNLE

UniProtKB: Peptidyl-prolyl cis-trans isomerase FKBP1B

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration9 mg/mL
BufferpH: 7.5
Component:
ConcentrationName
10.0 mMAtorvastatin
2.0 %DMSO
2.0 mMCaffeine
36.0 uMFree Ca2+
2.0 mMEGTA
25.0 mMTris
250.0 mMSodium Chloride
0.5 mMBenzamidine
0.5 mMTCEP
0.375 %CHAPS
0.001 %DOPC
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 25 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 3.9e-05 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: TFS Selectris
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 5007 / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: cryoSPARC (ver. 4.4.1) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionApplied symmetry - Point group: C4 (4 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 4.08 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.4.1) / Number images used: 22877
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.4.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.4.1)
FSC plot (resolution estimation)

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