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- EMDB-49537: Structure of mouse RyR1 with simvastatin (Ca2+/CFF/ATP dataset; c... -

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Basic information

Entry
Database: EMDB / ID: EMD-49537
TitleStructure of mouse RyR1 with simvastatin (Ca2+/CFF/ATP dataset; closed pore)
Map dataMouse RyR1 with simvastatin (Ca/CFF/ATP dataset; closed pore)
Sample
  • Complex: Complex of RyR1 with Calstabin-1 in presence of simvastatin (Ca2+/CFF/ATP condition)
    • Protein or peptide: Ryanodine receptor 1
    • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1A
  • Ligand: ZINC ION
  • Ligand: CAFFEINE
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: CALCIUM ION
  • Ligand: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: (1S,3R,7S,8S,8aR)-8-{2-[(2R,4R)-4-hydroxy-6-oxooxan-2-yl]ethyl}-3,7-dimethyl-1,2,3,7,8,8a-hexahydronaphthalen-1-yl 2,2-dimethylbutanoate
KeywordsCalcium / Ion Channel / TRANSPORT PROTEIN
Function / homology
Function and homology information


junctional membrane complex / TGF-beta receptor signaling activates SMADs / Calcineurin activates NFAT / mTORC1-mediated signalling / cytoplasmic side of membrane / regulation of muscle contraction / Stimuli-sensing channels / Ion homeostasis / heart trabecula formation / ryanodine-sensitive calcium-release channel activity ...junctional membrane complex / TGF-beta receptor signaling activates SMADs / Calcineurin activates NFAT / mTORC1-mediated signalling / cytoplasmic side of membrane / regulation of muscle contraction / Stimuli-sensing channels / Ion homeostasis / heart trabecula formation / ryanodine-sensitive calcium-release channel activity / terminal cisterna / ryanodine receptor complex / response to caffeine / release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / ossification involved in bone maturation / cellular response to caffeine / skin development / ventricular cardiac muscle tissue morphogenesis / FK506 binding / organelle membrane / smooth endoplasmic reticulum / outflow tract morphogenesis / regulation of ryanodine-sensitive calcium-release channel activity / T cell proliferation / heart morphogenesis / voltage-gated calcium channel activity / skeletal muscle fiber development / release of sequestered calcium ion into cytosol / T-tubule / sarcoplasmic reticulum membrane / muscle contraction / cellular response to calcium ion / sarcoplasmic reticulum / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / calcium channel activity / intracellular calcium ion homeostasis / cytokine-mediated signaling pathway / calcium ion transport / protease binding / protein homotetramerization / transmembrane transporter binding / calmodulin binding / calcium ion binding / synapse / enzyme binding / protein-containing complex / ATP binding / identical protein binding / membrane / cytosol
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 FKBP1A
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.6 Å
AuthorsWeninger G / Marks AR
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R01 HL145473 United States
CitationJournal: To Be Published
Title: Structural basis for statin-induced skeletal muscle weakness
Authors: Weninger G
History
DepositionMar 4, 2025-
Header (metadata) releaseOct 8, 2025-
Map releaseOct 8, 2025-
UpdateOct 8, 2025-
Current statusOct 8, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_49537.png

Downloads & links

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Map

FileDownload / File: emd_49537.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMouse RyR1 with simvastatin (Ca/CFF/ATP dataset; closed pore)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 512 pix.
= 424.448 Å		0.83 Å/pix.
x 512 pix.
= 424.448 Å		0.83 Å/pix.
x 512 pix.
= 424.448 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.829 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum0.0 - 0.7467636
Average (Standard dev.)0.0035301235 (±0.026749562)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 424.448 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_49537_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_49537_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Complex of RyR1 with Calstabin-1 in presence of simvastatin (Ca2+...

EntireName: Complex of RyR1 with Calstabin-1 in presence of simvastatin (Ca2+/CFF/ATP condition)
Components
  • Complex: Complex of RyR1 with Calstabin-1 in presence of simvastatin (Ca2+/CFF/ATP condition)
    • Protein or peptide: Ryanodine receptor 1
    • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1A
  • Ligand: ZINC ION
  • Ligand: CAFFEINE
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: CALCIUM ION
  • Ligand: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: (1S,3R,7S,8S,8aR)-8-{2-[(2R,4R)-4-hydroxy-6-oxooxan-2-yl]ethyl}-3,7-dimethyl-1,2,3,7,8,8a-hexahydronaphthalen-1-yl 2,2-dimethylbutanoate

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Supramolecule #1: Complex of RyR1 with Calstabin-1 in presence of simvastatin (Ca2+...

SupramoleculeName: Complex of RyR1 with Calstabin-1 in presence of simvastatin (Ca2+/CFF/ATP condition)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Details: 0.03 mM free Ca2+; 5 mM Caffeine; 10 mM ATP; 10 mM Simvastatin lactone
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: Ryanodine receptor 1

MacromoleculeName: Ryanodine receptor 1 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 565.692562 KDa
SequenceString: MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL EPTSNAQNVP PDLAICCFIL EQSLSVRALQ EMLANTVEA GVESSQGGGH RTLLYGHAIL LRHAHSRMYL SCLTTSRSMT DKLAFDVGLQ EDATGEACWW TMHPASKQRS E GEKVRVGD ...String:
MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL EPTSNAQNVP PDLAICCFIL EQSLSVRALQ EMLANTVEA GVESSQGGGH RTLLYGHAIL LRHAHSRMYL SCLTTSRSMT DKLAFDVGLQ EDATGEACWW TMHPASKQRS E GEKVRVGD DLILVSVSSE RYLHLSTASG ELQVDASFMQ TLWNMNPICS GCEEGFVTGG HVLRLFHGHM DECLTISPSD SD DQRRLVY YEGGPVCTHA RSLWRLEPLR ISWSGSHLRW GQPLRIRHVT TGRYLGLTED QGLVVVDASK AHTKATSFCF RIS KEKLDV APKRDVEGMG PPEIKYGESL CFVQHVASGL WLTYAAPDPK ALRLGVLKKK AMLHQEGHMD DALSLTRCQQ EESQ AARMI YSTAGLYNQF IKGLDSFSGK PRGSGPPAGS ALPIEGVILS LQDLIGYFEP PSEELQHEEK QTKLRSLRNR QSLFQ EEGM LSLVLNCIDR LNVYTTAAHF AEFAGEEAAE SWKEIVNLLY ELLASLIRGN RTNCALFSTN LDWLVSKLDR LEASSG ILE VLYCVLIESP EVLNIIQENH IKSIISLLDK HGRNHKVLDV LCSLCVCNGV AVRSNQDLIT ENLLPGRELL LQTNLIN YV TSIRPNIFVG RAEGSTQYGK WYFEVMVDEV APFLTAQATH LRVGWALSEG YSPYPGGGEG WGGNGVGDDL YSYGFDGL H LWTGHVARPV TSPGQHLLAP EDVVSCCLDL SVPSISFRIN GCPVQGVFES FNLDGLFFPV VSFSAGIKVR FLLGGRHGE FKFLPPPGYA PCHEAVLPRE RLHLQPIKEY RREGPRGPHL VGPSRCLSHL DFVPCPVDTI QIVLPPHLER IREKLAENIH ELWALTRIE QGWTYGPVRD DNKRLHPCLV NFHSLPEPER NYNLQMSGET LKTLLALGCH VGMADEKAED NLKKTKLPKT Y MMSNGYKP APLDLSHVRL TPAQTTLVDR LAENGHNVWA RDRVAQGWSY SAVQDIPARR NPRLVPYRLL DEATKRSNRD SL CQAVRTL LGYGYNIEPP DQEPSQVDSQ SRGDRARIFR AEKSYAVQSG RWYFEFEAVT TGEMRVGWAR PELRPDVELG ADD LAYVFN GHRGQRWHLG SEPFGRPWQS GDVVGCMIDL TENTIIFTLN GEVLMSDSGS ETAFRDIEIG DGFLPVCSLG PGQV GHLNL GQDVSSLRFF AICGLQEGFE PFAINMQRPV TTWFSKSLPQ FEPVPLEHPH YEVARMDGTV DTPPCLRLTH RTWGS QNSL VEMLFLRLSL PVQFHQHFRC TAGATPLASP GLQPPAEDEA RAAEPDTDYE NLRRSAGGWG EAEGGKDGTA KEGTPG GTA QAGVEAQPAR AENEKDATTE KNKKRGFLFK AKKVAMMTQP PSTPALPRLP RDVVPADNRD DPEIILNTTT YYYSVRV FA GQEPSCVWVG WVTPDYHQHD MSFDLSKVRA VTVTMGDEQG NVHSSLKCSN CYMVWGGDFV SPGQQGRISH TDLVIGCL V DLATGLMTFT ANGKESNTFF QVEPNTKLFP AVFVLPTHQN VVQFELGKQK NIMPLSAAMF LSERKNPAPQ CPPRLEVQM LMPVSWSRMP NHFLQVDTRR AGERLGWAVQ CQEPLMMMAL HIPEENRCMD ILELSERLDL QRFHSHTLSL YRSVCALGNN RVAHALCSH VDQAQLLHAL EDARLPGPLR AGYYDLLISI HLESACRSRR SMLSEYIVPL TPETRAITLF PPGRSAEDGP R RHGLPGVG VTTSLRPPHH FSPPCFVVAL PAAGATEAPA RLSPAIPLEA LRDKALRMLG EAVRDGGQHA RDPVGGSVEF QF VPVLKLV STLLVMGVFS DEDVKQILKM IEPEVFREEE EVEEEGEEEE EDEEEKEEDE EEEAHEKEDE EKEEAEDAAE EEK EELEEG LLQMKLPESV KLQMCHLLEY FCDQELQHRV ESLAAFAECY VDKMQGNQRG RYGLLMKAFT MSAAETARRT REFR SPPQE QINMLLHFKN GADEEECPLP EEIRQELVNF HQDLLAHCGI QLEGEEEEPE EESTLGSRLM SLLEKVKLVK KTEEK PEEE PAPEEHKPQS LQELVSHTVV RWAQEDFVQS PELVRAMFSL LHRQYDGLGE LLRALPRAYT ISVSSVEDTM SLLECL GQI RSLLIVQMGP QEENLMIQSI GNIMNNKVFY QHPNLMRALG MHETVMEVMV NVLGGGESKE IRFPKMVTSC CRFLCYF CR ISRQNQRSMF DHLSYLLENS GIGLGMQGST PLDVAAASVI DNNELALALQ EQDLEKVVSY LAGCGLQSCP MLLAKGYP D IGWNPCGGER YLDFLRFAVF VNGESVEENA NVVVRLLIRK PECFGPALRG EGGSGLLAAI EEAIRISEDP ARDGPGVRR DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE THLIQAGKGE ALRIRAILRS LVPLDDLVGI ISLPLQIPTL GKDGALVQP KMSASFVPDH KASMVLFLDR VYGIENQDFL LHVLDVGFLP DMRAAASLDT ATFSTTEMAL ALNRYLCLAV L PLITKCAP LFAGTEHRAI MVDSMLHTVY RLSRGRSLTK AQRDVIEDCL MALCRYIRPS MLQHLLRRLV FDVPILNEFA KM PLKLLTN HYERCWKYYC LPTGWANFGV TSEEELHLTR KLFWGIFDSL AHKKYDQELY RIAMPCLCAI AGALPPDYVD ASY SSKTEK KATVDAEGNF DPRPVETLNV IIPEKLDSFI NKFAEYTHEK WAFDKIQNNW SYGENIDEEL KTHPMLRPYK TFSE KDKEI YRWPIKESLK AMIAWEWTVE KAREGEEEKT EKKKTRKISQ TAQTYDPREG YNPQPPDLSV VTLSRELQAM AEQLA ENYH NTWGRKKKQE LEAKGGGSHP LLVPYDTLTA KEKARDREKA QELLKFLQMN GYAVTRGLKD MELDTSSIEK RFAFGF LQQ LLRWMDISQE FIAHLEAVVS SGRVEKSPHE QEIKFFAKIL LPLINQYFTN HCLYFLSTPA KVLGSGGHAS NKEKEMI TS LFCKLAALVR HRVSLFGTDA PAVVNCLHIL ARSLDARTVM KSGPEIVKAG LRSFFESASE DIEKMVENLR LGKVSQAR T QVKGVGQNLT YTTVALLPVL TTLFQHIAQH QFGDDVILDD VQVSCYRTLC SIYSLGTTRN PYVEKLRPAL GECLARLAA AMPVAFLEPE LNEYNACSVY TTKSPRERAI LGLPNSVEEM CPDIPVLERL MAEIGGLAES GARYTEMPHV IEITLPMLCS YLPRWWERG PEAPPPALPA GAPPPCTAVT SDHLNSLLGN ILRIIVNNLG IDEASWMKRL AVFAQPIVSR ARPELLRSHF I PTIGRLRK RAGKVVAEEE QLRLEAKAEA EEGELLVRDE FSVLCRDLYA LYPLLIRYVD NNRAHWLTEP NPNAEELFRM VG EIFIYWS KSHNFKREEQ NFVVQNEINN MSFLTADNKS KMAKAGDVQS GGSDQERTKK KRRGDRYSVQ TSLIVATLKK MLP IGLNMC APTDQDLIVL AKARYALKDT DEEVREFLQN NLNLQGKVEG SPSLRWQMAL YRGVPGREED ADDPEKIVRR VQEV SAVLY HLDQTEHPYK SKKAVWHKLL SKQRRRAVVA CFRMTPLYNL PTHRACNMFL ESYKASWILT EDHSFEDRMI DDLSK AGEQ EEEEEEVEEK KPDPLHQLVL HFSRTALTEK SKLDEDYLYM AYADIMAKSC HLEEGGENGE EGGEEEEVEV SFEEKE MEK QRLLYQQSRL HNRGAAEMVL QMISACKGET GAMVSSTLKL GISILNGGNA EVQQKMLDYL KDKKEVGFFQ SIQALMQ TC SVLDLNAFER QNKAEGLGMV NEDGTVINRQ NGEKVMADDE FTQDLFRFLQ LLCEGHNNDF QNYLRTQTGN TTTINIII C TVDYLLRLQE SISDFYWYYS GKDVIEEQGK RNFSKAMSVA KQVFNSLTEY IQGPCTGNQQ SLAHSRLWDA VVGFLHVFA HMMMKLAQDS SQIELLKELL DLQKDMVVML LSLLEGNVVN GMIARQMVDM LVESSSNVEM ILKFFDMFLK LKDIVGSEAF QDYVTDPRG LISKKDFQKA MDSQKQFTGP EIQFLLSCSE ADENEMINCE EFANRFQEPA RDIGFNVAVL LTNLSEHVPH D PRLRNFLE LAESILEYFR PYLGRIEIMG ASRRIERIYF EISETNRAQW EMPQVKESKR QFIFDVVNEG GESEKMEMFV SF CEDTIFE MQIAAQISEP EGEPEEDEDE GAEEAEEGAA GSDGSGSAAA AGVWVWLAAT AGRTLRGLSY RSLRRRVRRL RRL TAREAA TAVAALLWAL VTRAGGAGAG AAAGALRLLW GSLFGGGLVD SAKKVTVTEL LAGMPDPTGD EVHGQQPSGA GSDA EGEGE GEGEGDAADG AGDEEAAADQ AGTGGADGAV AVADGSPFRP EGAGGLGDMG DTTPVEPPTP EGSPILKRKL GVDGE EEEP PPEPEPEPEP EPEKADTENG EKEVPEPPPE PPKKTPPPPP PKKEEAGGAG LEEFWGELEV QRVKFLNYLS RNFYTL RFL ALFLAFAINF ILLFYKVSDS PPGEDDIEGS GAGDMSGAGS GDGSGWGSRA GEEVEGDEDE NMVYYFLEES TGYMEPA LR CLSLLHTLVA FLCIIGYNCL KVPLVIFKRE KELARKLEFD GLYITEQPED DDVKGQWDRL VLNTPSFPSN YWDKFVKR K VLDKHGDIFG RERIAELLGM DLASLEITAH NERKPDPPPG LLTWIMSIDV KYQIWKFGVI FTDNSFLYLG WYMVMSLLG HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT VVAFNFFRKF YNKSEDEDEP DMKCDDMMTC YLFHMYVGV RAGGGIGDEI EDPAGDEYEL YRVVFDITFF FFVIVILLAI IQGLIIDAFG ELRDQQEQVK EDMETKCFIC G IGSDYFDT TPHGFETHTL EEHNLANYMF FLMYLINKDE TEHTGQESYV WKMYQERCWD FFPAGDCFRK QYEDQLS

UniProtKB: Ryanodine receptor 1

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Macromolecule #2: Peptidyl-prolyl cis-trans isomerase FKBP1A

MacromoleculeName: Peptidyl-prolyl cis-trans isomerase FKBP1A / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 11.939629 KDa
SequenceString:
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT LGKQEVIRGW EEGVAQMSVG QRAKLIISSD YAYGATGHP GIIPPHATLV FDVELLKLE

UniProtKB: Peptidyl-prolyl cis-trans isomerase FKBP1A

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Macromolecule #3: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 3 / Number of copies: 4 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #4: CAFFEINE

MacromoleculeName: CAFFEINE / type: ligand / ID: 4 / Number of copies: 4 / Formula: CFF
Molecular weightTheoretical: 194.191 Da
Chemical component information

ChemComp-CFF:
CAFFEINE / medication*YM

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Macromolecule #5: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 8 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #6: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 6 / Number of copies: 4 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #7: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 7 / Number of copies: 8 / Formula: PCW
Molecular weightTheoretical: 787.121 Da
Chemical component information

ChemComp-PCW:
1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipid*YM

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Macromolecule #8: (1S,3R,7S,8S,8aR)-8-{2-[(2R,4R)-4-hydroxy-6-oxooxan-2-yl]ethyl}-3...

MacromoleculeName: (1S,3R,7S,8S,8aR)-8-{2-[(2R,4R)-4-hydroxy-6-oxooxan-2-yl]ethyl}-3,7-dimethyl-1,2,3,7,8,8a-hexahydronaphthalen-1-yl 2,2-dimethylbutanoate
type: ligand / ID: 8 / Number of copies: 8 / Formula: A1BYZ
Molecular weightTheoretical: 418.566 Da

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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

Concentration8.5 mg/mL
BufferpH: 7.4
Component:
ConcentrationNameFormula
10.0 mmol/LHEPES
400.0 mmol/Lsodium chlorideNaCl
1.0 mmol/LEGTA
0.25 %CHAPS
0.01 %DOPC
0.5 mmol/LTCEP
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 2 / Number real images: 7207 / Average electron dose: 58.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.2 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 / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL / In silico model: CryoSPARC ab initio
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 65309
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC / Details: CryoSPARC branch-and-bound
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC / Details: CryoSPARC branch-and-bound
FSC plot (resolution estimation)

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