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- EMDB-27711: Recombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D... -

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Basic information

Entry
Database: EMDB / ID: EMD-27711
TitleRecombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D/S2030D in complex with FKBP12.6 and nanodisc under closed-state conditions
Map data
Sample
  • Complex: Recombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D/S2030D in complex with FKBP12.6 and nanodisc under closed-state conditions
    • Protein or peptide: Ryanodine receptor 2
    • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B
  • Ligand: ZINC ION
KeywordsRyanodine receptor / Calcium channel / Mutation / Triple mutant / RyR2 / Phosphorylation / MEMBRANE PROTEIN
Function / homology
Function and homology information


manganese ion transmembrane transport / suramin binding / establishment of protein localization to endoplasmic reticulum / type B pancreatic cell apoptotic process / Purkinje myocyte to ventricular cardiac muscle cell signaling / regulation of SA node cell action potential / regulation of atrial cardiac muscle cell action potential / left ventricular cardiac muscle tissue morphogenesis / organic cyclic compound binding / regulation of AV node cell action potential ...manganese ion transmembrane transport / suramin binding / establishment of protein localization to endoplasmic reticulum / type B pancreatic cell apoptotic process / Purkinje myocyte to ventricular cardiac muscle cell signaling / regulation of SA node cell action potential / regulation of atrial cardiac muscle cell action potential / left ventricular cardiac muscle tissue morphogenesis / organic cyclic compound binding / regulation of AV node cell action potential / calcium-induced calcium release activity / sarcoplasmic reticulum calcium ion transport / Stimuli-sensing channels / Ion homeostasis / ventricular cardiac muscle cell action potential / regulation of ventricular cardiac muscle cell action potential / positive regulation of sequestering of calcium ion / cyclic nucleotide binding / embryonic heart tube morphogenesis / negative regulation of release of sequestered calcium ion into cytosol / negative regulation of insulin secretion involved in cellular response to glucose stimulus / regulation of cardiac muscle contraction by calcium ion signaling / cardiac muscle hypertrophy / ryanodine-sensitive calcium-release channel activity / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / response to muscle activity / calcium ion transmembrane import into cytosol / calcium ion transport into cytosol / A band / response to caffeine / cell communication by electrical coupling involved in cardiac conduction / response to redox state / protein maturation by protein folding / 'de novo' protein folding / negative regulation of heart rate / negative regulation of phosphoprotein phosphatase activity / positive regulation of heart rate / FK506 binding / negative regulation of cytosolic calcium ion concentration / positive regulation of axon regeneration / cellular response to caffeine / protein kinase A regulatory subunit binding / smooth endoplasmic reticulum / intracellularly gated calcium channel activity / protein kinase A catalytic subunit binding / positive regulation of the force of heart contraction / response to magnesium ion / : / detection of calcium ion / smooth muscle contraction / striated muscle contraction / negative regulation of ryanodine-sensitive calcium-release channel activity / response to vitamin E / regulation of cardiac muscle contraction / calcium channel inhibitor activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / protein peptidyl-prolyl isomerization / T cell proliferation / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / release of sequestered calcium ion into cytosol / Ion homeostasis / regulation of ryanodine-sensitive calcium-release channel activity / cardiac muscle contraction / sarcoplasmic reticulum membrane / cellular response to epinephrine stimulus / calcium channel complex / regulation of cytosolic calcium ion concentration / response to muscle stretch / extrinsic component of cytoplasmic side of plasma membrane / regulation of heart rate / sarcomere / monoatomic ion transmembrane transport / sarcoplasmic reticulum / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / establishment of localization in cell / calcium-mediated signaling / calcium ion transmembrane transport / sarcolemma / response to hydrogen peroxide / calcium channel activity / Stimuli-sensing channels / intracellular calcium ion homeostasis / Z disc / response to calcium ion / : / calcium ion transport / nuclear envelope / positive regulation of cytosolic calcium ion concentration / protein refolding / scaffold protein binding / transmembrane transporter binding / response to hypoxia / calmodulin binding / signaling receptor binding / calcium ion binding / protein kinase binding / enzyme binding
Similarity search - Function
: / Ryanodine receptor junctional solenoid repeat / Ryanodine receptor, SPRY domain 2 / 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 junctional solenoid repeat / Ryanodine receptor, SPRY domain 2 / 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. / SPRY domain / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase / Peptidyl-prolyl cis-trans isomerase domain superfamily / EF-hand domain pair / EF-hand domain / Ion transport domain / Ion transport protein / EF-hand domain pair / Concanavalin A-like lectin/glucanase domain superfamily
Similarity search - Domain/homology
Ryanodine receptor 2 / Peptidyl-prolyl cis-trans isomerase FKBP1B
Similarity search - Component
Biological speciesMus musculus (house mouse) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsIyer KA / Hu Y / Murayama T / Samso M
Funding support United States, 5 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)R01 AR068431 United States
American Heart Association19POST34430178 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)HSSN26120080001E United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24 GM116789 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24 GM116790 United States
CitationJournal: To Be Published
Title: Recombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D/S2030D in complex with FKBP12.6 and nanodisc under closed-state conditions
Authors: Hu Y / Iyer KA / Nayak AR / Eltit JM / Kurebayashi N / Murayama T / Samso M
History
DepositionJul 26, 2022-
Header (metadata) releaseJan 31, 2024-
Map releaseJan 31, 2024-
UpdateJan 31, 2024-
Current statusJan 31, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_27711.png

Downloads & links

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Map

FileDownload / File: emd_27711.map.gz / Format: CCP4 / Size: 371.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.08 Å
Density
Contour LevelBy AUTHOR: 0.24
Minimum - Maximum-1.4576077 - 2.8039804
Average (Standard dev.)0.0026045844 (±0.06471021)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions460460460
Spacing460460460
CellA=B=C: 496.80002 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_27711_additional_1.map
Projections & Slices
AxesZYX

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Half map: #2

Fileemd_27711_half_map_1.map
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Half map: #1

Fileemd_27711_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : Recombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D...

EntireName: Recombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D/S2030D in complex with FKBP12.6 and nanodisc under closed-state conditions
Components
  • Complex: Recombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D/S2030D in complex with FKBP12.6 and nanodisc under closed-state conditions
    • Protein or peptide: Ryanodine receptor 2
    • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B
  • Ligand: ZINC ION

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Supramolecule #1: Recombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D...

SupramoleculeName: Recombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D/S2030D in complex with FKBP12.6 and nanodisc under closed-state conditions
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 2.26 MDa

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Macromolecule #1: Ryanodine receptor 2

MacromoleculeName: Ryanodine receptor 2 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 565.62 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP DLSICTFVLE QSLSVRALQE MLANTVEKS EGQVDVEKWK FMMKTAQGGG HRTLLYGHAI LLRHSYSGMY LCCLSTSRSS TDKLAFDVGL QEDTTGEACW W TIHPASKQ ...String:
MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP DLSICTFVLE QSLSVRALQE MLANTVEKS EGQVDVEKWK FMMKTAQGGG HRTLLYGHAI LLRHSYSGMY LCCLSTSRSS TDKLAFDVGL QEDTTGEACW W TIHPASKQ RSEGEKVRVG DDLILVSVSS ERYLHLSYGN SSWHVDAAFQ QTLWSVAPIS SGSEAAQGYL IGGDVLRLLH GH MDECLTV PSGEHGEEQR RTVHYEGGAV SVHARSLWRL ETLRVAWSGS HIRWGQPFRL RHVTTGKYLS LMEDKNLLLM DKE KADVKS TAFAFRSSKE KLDVGVRKEV DGMGTSEIKY GDSICYIQHV DTGLWLTYQA VDVKSARMGS IQRKAIMHHE GHMD DGLNL SRSQHEESRT ARVIRSTVFL FNRFIRGLDA LSKKVKLPTI DLPIESVSLS LQDLIGYFHP PDEHLEHEDK QNRLR ALKN RQNLFQEEGM INLVLECIDR LHVYSSAAHF ADVAGREAGE SWKSILNSLY ELLAALIRGN RKNCAQFSGS LDWLIS RLE RLEASSGILE VLHCVLVESP EALNIIKEGH IKSIISLLDK HGRNHKVLDV LCSLCVCHGV AVRSNQHLIC DNLLPGR DL LLQTRLVNHV SSMRPNIFLG VSEGSAQYKK WYYELMVDHT EPFVTAEATH LRVGWASTEG YSPYPGGGEE WGGNGVGD D LFSYGFDGLH LWSGCIARTV SSPNQHLLRT DDVISCCLDL SAPSISFRIN GQPVQGMFEN FNIDGLFFPV VSFSAGIKV RFLLGGRHGE FKFLPPPGYA ACYEAVLPKE KLKVEHSREY KQERTYTRDL LGPTVSLTQA AFTPVPVDTS QIVLPPHLER IRERLAENI HELWVMNKIE LGWQYGPVRD DNKRQHPCLV EFCKLPEQER NYNLQMSLET LKTLLALGCH VGIADEHAEE K VKKMKLPK NYQLTSGYKP APMDLSFIKL TPSQEAMVDK LAENAHNVWA RDRIRQGWTY GIQQDVKNRR NPRLVPYTLL DD RTKKSNK DSLREAVRTL LGYGYHLEAP DQDHASRAEV CSGTGERFRI FRAEKTYAVK AGRWYFEFEA VTAGDMRVGW SRP GCQPDL ELGSDDRAFA FDGFKAQRWH QGNEHYGRSW QAGDVVGCMV DMNEHTMMFT LNGEILLDDS GSELAFKDFD VGDG FIPVC SLGVAQVGRM NFGKDVSTLK YFTICGLQEG YEPFAVNTNR DITMWLSKRL PQFLQVPSNH EHIEVTRIDG TIDSS PCLK VTQKSFGSQN NNTDIMFYRL SMPIECAEVF SKSVAGGLPG AGFYGPKNDL EDFDVDSDFE VLMKTAHGHL VPDRID KDK ETPKPEFNNH KDYAQEKPSR LKQRFLLRRT KPDYSTGHSA RLTEDVLADD RDDYEYLMQT STYYYSVRIF PGQEPAN VW VGWITSDFHQ YDTGFDLDRV RTVTVTLGDE KGKVHESIKR SNCYMVCAGE SMSPGQGRNN SNGLEIGCVV DAASGLLT F IANGKELSTY YQVEPSTKLF PAVFAQATSP NVFQFELGRI KNVMPLSAGL FKSEHKNPVP QCPPRLHVQF LSHVLWSRM PNQFLKVDVS RISERQGWLV QCLDPLQFMS LHIPEENRSV DILELTEQEE LLQFHYHTLR LYSAVCALGN HRVAHALCSH VDEPQLLYA IENKYMPGLL RAGYYDLLID IHLSSYATAR LMMNNEFIVP MTEETKSITL FPDENKKHGL PGIGLSTSLR P RMRFSSPS FVSISNDCYQ YSPEFPLDIL KAKTIQMLTE AVKEGSLHAR DPVGGTTEFL FVPLIKLFYT LLIMGIFHNE DL KHILQLI EPSVFKEAAV PEEEGGTPEK EISIEDAKLE GEEEAKGGKR PKEGLLQMKL PEPVKLQMCL LLQYLCDCQV RHR IEAIVA FSDDFVAKLQ DNQRFRYNEV MQALNMSAAL TARKTREFRS PPQEQINMLL NFKDDKSECP CPEEIRDQLL DFHE DLMTH CGIELDEDGS LDGSNDLTIR GRLLDLVEKV TYLKKKQAEK PVASDSRKCS SLQQLISETM VRWAQESVIE DPELV RAMF VLLHRQYDGI GGLVRALPKT YTINGVSVED TINLLASLGQ IRSLLSVRMG KEEEKLMIRG LGDIMNNKVF YQHPNL MRA LGMHETVMEV MVNVLGGGES KEITFPKMVA NCCRFLCYFC RISRQNQKAM FDHLSYLLEN SSVGLASPAM RGSTPLD VA AASVMDNNEL ALALREPDLE KVVRYLAGCG LQSCQMLVSK GYPDIGWNPV EGERYLDFLR FAVFCNGESV EENANVVV R LLIRRPECFG PALRGEGGNG LLAAMEEAIK IAEDPSRDGP SPTSGSSKTL DIEEEEDDTI HMGNAIMTFY AALIDLLGR CAPEMHLIHA GKGEAIRIRS ILRSLIPLGD LVGVISIAFQ MPTIAKDGKV VEPDMSAGFC PDHKAAMVLF LDRVYGIEVQ DFLLHLLEV GFLPDLRAAA SLDTAALSAT DMALALNRYL CTAVLPLLTR CAPLFAGTEH HASLIDSLLH TVYRLSKGCS L TKAQRDSI EVCLLSICGQ LRPSMMQHLL RRLVFDVPLL NEHAKMPLKL LTNHYERCWK YYCLPGGWGN FGAASEEELH LS RKLFWGI FDALSQKKYE QELFKLALPC LSAVAGALPP DYMESNYVSM MEKQSSMDSE GNFNPQPVDT SNITIPEKLE YFI NKYAEH SHDKWSMDKL ANGWIYGEIY SDSSKIQPLM KPYKLLSEKE KEIYRWPIKE SLKTMLAWGW RIERTREGDS MALY NRTRR IDQTSQVDID AAHGYSPRAI DMSNVTLSRD LHAMAEMMAE NYHNIWAKKK KLELESKGGG NHPLLVPYDT LTAKE KAKD REKAQDIFKF LQISGYVVSR GFKDLDLDTP SIEKRFAYSF LQQLIRYVDE AHQYILEFDG GSRSKGEHFP YEQEIK FFA KVVLPLIDQY FKNHRLYFLS AASRPLCTGG HASNKEKEMV TSLFCKLGVL VRHRISLFGN DATSIVNCLH ILGQTLD AR TVMKTGLDSV KSALRAFLDN AAEDLEKTME NLKQGQFTHT RSQPKGVTQI INYTTVALLP MLSSLFEHIG QHQFGEDL I LEDVQVSCYR ILTSLYALGT SKSIYVERQR SALGECLAAF AGAFPIAFLE THLDKHNVYS IYNTRSSRER AALSLPANV EDVCPNIPSL EKLMTEIIEL AESGIRYTQM PYMMEVVLPM LCSYMSRWWE HGPENHPERA EMCCTALNSE HMNTLLGNIL KIIYNNLGI DEGAWMKRLA VFSQPIINKV KPQLLKTHFL PLMEKLKKKA AMVVSEEDHL KAEARGDMSE AELLILDEFT T LARDLYAF YPLLIRFVDY NRAKWLKEPN PEAEELFRMV AEVFIYWSKS HNFKREEQNF VVQNEINNMS FLITDTKSKM SK AAISDQE RKKMKRKGDR YSMQTSLIVA ALKRLLPIGL NICAPGDQEL IALAKNRFSL KDTEEEVRDI IRSNIHLQGK LED PAIRWQ MALYKDLPNR TEDPSDPERT VERVLGIANV LFHLEQKSKY TGRGYFSLVE HPQRSKKAVW HKLLSKQRKR AVVA CFRMA PLYNLPRHRA VNLFLQGYEK SWIETEEHYF EDKLIEDLAK PGAELPEEDE AMKRVDPLHQ LILLFSRTAL TEKCK LEED FLYMAYADIM AKSCHDEEDD DGEEEVKSFE EKEMEKQKLL YQQARLHDRG AAEMVLQTIS ASKGETGPMV AATLKL GIA ILNGGNSTVQ QKMLDYLKEK KDVGFFQSLA GLMQSCSVLD LNAFERQNKA EGLGMVTEEG SGEKVLQDDE FTCDLFR FL QLLCEGHNSD FQNYLRTQTG NNTTVNIIIS TVDYLLRVQE SISDFYWYYS GKDIIDEQGQ RNFSKAIQVA KQVFNTLT E YIQGPCTGNQ QSLAHSRLWD AVVGFLHVFA HMQMKLSQDS SQIELLKELM DLQKDMVVML LSMLEGNVVN GTIGKQMVD MLVESSNNVE MILKFFDMFL KLKDLTSSDT FKEYDPDGKG VISKRDFHKA MESHKHYTQS ETEFLLSCAE TDENETLDYE EFVKRFHEP AKDIGFNVAV LLTNLSEHMP NDTRLQTFLE LAESVLNYFQ PFLGRIEIMG SAKRIERVYF EISESSRTQW E KPQVKESK RQFIFDVVNE GGEKEKMELF VNFCEDTIFE MQLAAQISES DLNERLANKE ESEKERPEEQ APRMGFFSLL TI QSALFAL RYNVLTLVRM LSLKSLKKQM KRMKKMTVKD MVLAFFSSYW SVFVTLLHFV ASVCRGFFRI VSSLLLGGSL VEG AKKIKV AELLANMPDP TQDEVRGDEE EGERKPLESA LPSEDLTDLK ELTEESDLLS DIFGLDLKRE GGQYKLIPHN PNAG LSDLM TNPVPVPEVQ EKFQEQKAKE EKEEKEETKS EPEKAEGEDG EKEEKAKDEK SKQKLRQLHT HRYGEPEVPE SAFWK KIIA YQQKLLNYFA RNFYNMRMLA LFVAFAINFI LLFYKVSTSS VVEGKELPTR TSSDTAKVTN SLDSSPHRII AVHYVL EES SGYMEPTLRI LAILHTIISF FCIIGYYCLK VPLVIFKREK EVARKLEFDG LYITEQPSED DIKGQWDRLV INTQSFP NN YWDKFVKRKV MDKYGEFYGR DRISELLGMD KAALDFSDAR EKKKPKKDSS LSAVLNSIDV KYQMWKLGVV FTDNSFLY L AWYMTMSVLG HYNNFFFAAH LLDIAMGFKT LRTILSSVTH NGKQLVLTVG LLAVVVYLYT VVAFNFFRKF YNKSEDGDT PDMKCDDMLT CYMFHMYVGV RAGGGIGDEI EDPAGDEYEI YRIIFDITFF FFVIVILLAI IQGLIIDAFG ELRDQQEQVK EDMETKCFI CGIGNDYFDT VPHGFETHTL QEHNLANYLF FLMYLINKDE TEHTGQESYV WKMYQERCWE FFPAGDCFRK Q YEDQLN

UniProtKB: Ryanodine receptor 2

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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 / Number of copies: 4 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.667305 KDa
Recombinant expressionOrganism: Escherichia coli BL21 (bacteria)
SequenceString:
GVEIETISPG DGRTFPKKGQ TCVVHYTGML QNGKKFDSSR DRNKPFKFRI GKQEVIKGFE EGAAQMSLGQ RAKLTCTPDV AYGATGHPG VIPPNATLIF DVELLNLE

UniProtKB: Peptidyl-prolyl cis-trans isomerase FKBP1B

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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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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration3.8 mg/mL
BufferpH: 7.4
Component:
ConcentrationFormulaName
20.0 mMMOPS3-(N-Morpholino)propanesulfonic acid sodium salt
0.6 MKClPotassium Chloride
2.0 mMDTTDithiothreitol
2.0 mMEGTAEthyleneglycol-bis(beta-aminoethyl ether)-N,N,N,N-tetraacetic Acid
GridModel: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 81000
Specialist opticsEnergy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 2 / Number real images: 6274 / Average exposure time: 4.16 sec. / Average electron dose: 52.95 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 617802
Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.1)
Final angle assignmentType: PROJECTION MATCHING / Software - Name: cryoSPARC (ver. 3.1)
Final reconstructionApplied symmetry - Point group: C4 (4 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.1) / Number images used: 406681
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6wou


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-8dty:
Recombinant mouse RyR2 triple phosphomimetic mutant S2807D/S2813D/S2030D in complex with FKBP12.6 and nanodisc under closed-state conditions

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