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- EMDB-23868: Human N-type voltage-gated calcium channel Cav2.2 at 3.1 Angstrom... -

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Basic information

Entry
Database: EMDB / ID: EMD-23868
TitleHuman N-type voltage-gated calcium channel Cav2.2 at 3.1 Angstrom resolution
Map data
Sample
  • Complex: Cav2.2N-type calcium channel
    • Protein or peptide: Voltage-dependent N-type calcium channel subunit alpha-1B
    • Protein or peptide: Voltage-dependent L-type calcium channel subunit beta-3
    • Protein or peptide: Voltage-dependent calcium channel subunit alpha-2/delta-1Voltage-gated calcium channel
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: CALCIUM IONCalcium
  • Ligand: CHOLESTEROL HEMISUCCINATE
  • Ligand: CHOLESTEROL
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate
Function / homology
Function and homology information


regulation of membrane repolarization during action potential / Presynaptic depolarization and calcium channel opening / positive regulation of high voltage-gated calcium channel activity / calcium ion transmembrane transport via high voltage-gated calcium channel / membrane depolarization during bundle of His cell action potential / L-type voltage-gated calcium channel complex / cardiac muscle cell action potential involved in contraction / high voltage-gated calcium channel activity / NCAM1 interactions / regulation of ventricular cardiac muscle cell membrane repolarization ...regulation of membrane repolarization during action potential / Presynaptic depolarization and calcium channel opening / positive regulation of high voltage-gated calcium channel activity / calcium ion transmembrane transport via high voltage-gated calcium channel / membrane depolarization during bundle of His cell action potential / L-type voltage-gated calcium channel complex / cardiac muscle cell action potential involved in contraction / high voltage-gated calcium channel activity / NCAM1 interactions / regulation of ventricular cardiac muscle cell membrane repolarization / calcium ion transport into cytosol / regulation of calcium ion transmembrane transport via high voltage-gated calcium channel / neuromuscular junction development / voltage-gated calcium channel complex / neuronal dense core vesicle / regulation of heart rate by cardiac conduction / calcium ion import across plasma membrane / calcium channel regulator activity / regulation of calcium ion transport / response to amyloid-beta / voltage-gated calcium channel activity / sarcoplasmic reticulum / Regulation of insulin secretion / protein localization to plasma membrane / modulation of chemical synaptic transmission / Adrenaline,noradrenaline inhibits insulin secretion / cellular response to amyloid-beta / calcium ion transport / amyloid-beta binding / T cell receptor signaling pathway / chemical synaptic transmission / neuronal cell body / synapse / calcium ion binding / extracellular exosome / ATP binding / membrane / metal ion binding / plasma membrane / cytosol
Similarity search - Function
Voltage-dependent calcium channel, N-type, alpha-1 subunit / Voltage-dependent calcium channel, L-type, beta-3 subunit / Voltage-dependent L-type calcium channel subunit beta-3, SH3 domain / Voltage-dependent L-type calcium channel subunit beta-1-4, N-terminal A domain / Voltage-dependent calcium channel, L-type, beta subunit / Voltage gated calcium channel subunit beta domain 4Aa N terminal / VWA N-terminal / Voltage-dependent calcium channel, alpha-2/delta subunit, conserved region / VWA N-terminal / Neuronal voltage-dependent calcium channel alpha 2acd ...Voltage-dependent calcium channel, N-type, alpha-1 subunit / Voltage-dependent calcium channel, L-type, beta-3 subunit / Voltage-dependent L-type calcium channel subunit beta-3, SH3 domain / Voltage-dependent L-type calcium channel subunit beta-1-4, N-terminal A domain / Voltage-dependent calcium channel, L-type, beta subunit / Voltage gated calcium channel subunit beta domain 4Aa N terminal / VWA N-terminal / Voltage-dependent calcium channel, alpha-2/delta subunit, conserved region / VWA N-terminal / Neuronal voltage-dependent calcium channel alpha 2acd / Voltage-dependent calcium channel, alpha-1 subunit, IQ domain / Voltage gated calcium channel IQ domain / Voltage gated calcium channel IQ domain / Voltage-dependent calcium channel, alpha-1 subunit / Voltage-dependent L-type calcium channel, IQ-associated domain / Voltage-dependent L-type calcium channel, IQ-associated / Guanylate kinase/L-type calcium channel beta subunit / Guanylate kinase / Guanylate kinase homologues. / von Willebrand factor type A domain / von Willebrand factor (vWF) type A domain / VWFA domain profile. / Voltage-dependent channel domain superfamily / von Willebrand factor, type A / von Willebrand factor A-like domain superfamily / EF-hand calcium-binding domain profile. / SH3-like domain superfamily / Ion transport domain / Ion transport protein / Src homology 3 (SH3) domain profile. / SH3 domain / EF-hand domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Voltage-dependent L-type calcium channel subunit beta-3 / Voltage-dependent calcium channel subunit alpha-2/delta-1 / Voltage-dependent N-type calcium channel subunit alpha-1B
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsYan N / Gao S / Yao X
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)5R01GM130762 United States
CitationJournal: Nature / Year: 2021
Title: Structure of human Ca2.2 channel blocked by the painkiller ziconotide.
Authors: Shuai Gao / Xia Yao / Nieng Yan /
Abstract: The neuronal-type (N-type) voltage-gated calcium (Ca) channels, which are designated Ca2.2, have an important role in the release of neurotransmitters. Ziconotide is a Ca2.2-specific peptide pore ...The neuronal-type (N-type) voltage-gated calcium (Ca) channels, which are designated Ca2.2, have an important role in the release of neurotransmitters. Ziconotide is a Ca2.2-specific peptide pore blocker that has been clinically used for treating intractable pain. Here we present cryo-electron microscopy structures of human Ca2.2 (comprising the core α1 and the ancillary α2δ-1 and β3 subunits) in the presence or absence of ziconotide. Ziconotide is thoroughly coordinated by helices P1 and P2, which support the selectivity filter, and the extracellular loops (ECLs) in repeats II, III and IV of α1. To accommodate ziconotide, the ECL of repeat III and α2δ-1 have to tilt upward concertedly. Three of the voltage-sensing domains (VSDs) are in a depolarized state, whereas the VSD of repeat II exhibits a down conformation that is stabilized by Ca2-unique intracellular segments and a phosphatidylinositol 4,5-bisphosphate molecule. Our studies reveal the molecular basis for Ca2.2-specific pore blocking by ziconotide and establish the framework for investigating electromechanical coupling in Ca channels.
History
DepositionApr 18, 2021-
Header (metadata) releaseJul 7, 2021-
Map releaseJul 7, 2021-
UpdateAug 18, 2021-
Current statusAug 18, 2021Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.023
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.023
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7miy
  • Surface level: 0.023
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_23868.png

Downloads & links

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Map

FileDownload / File: emd_23868.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.114 Å
Density
Contour LevelBy AUTHOR: 0.023 / Movie #1: 0.023
Minimum - Maximum-0.10476063 - 0.1651723
Average (Standard dev.)1.250235e-05 (±0.0054037846)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 311.91998 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.1141.1141.114
M x/y/z280280280
origin x/y/z0.0000.0000.000
length x/y/z311.920311.920311.920
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ256256256
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS280280280
D min/max/mean-0.1050.1650.000

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Supplemental data

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Sample components

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Entire : Cav2.2

EntireName: Cav2.2N-type calcium channel
Components
  • Complex: Cav2.2N-type calcium channel
    • Protein or peptide: Voltage-dependent N-type calcium channel subunit alpha-1B
    • Protein or peptide: Voltage-dependent L-type calcium channel subunit beta-3
    • Protein or peptide: Voltage-dependent calcium channel subunit alpha-2/delta-1Voltage-gated calcium channel
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: CALCIUM IONCalcium
  • Ligand: CHOLESTEROL HEMISUCCINATE
  • Ligand: CHOLESTEROL
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate

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Supramolecule #1: Cav2.2

SupramoleculeName: Cav2.2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)

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Macromolecule #1: Voltage-dependent N-type calcium channel subunit alpha-1B

MacromoleculeName: Voltage-dependent N-type calcium channel subunit alpha-1B
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 262.831781 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MVRFGDELGG RYGGPGGGER ARGGGAGGAG GPGPGGLQPG QRVLYKQSIA QRARTMALYN PIPVKQNCFT VNRSLFVFSE DNVVRKYAK RITEWPPFEY MILATIIANC IVLALEQHLP DGDKTPMSER LDDTEPYFIG IFCFEAGIKI IALGFVFHKG S YLRNGWNV ...String:
MVRFGDELGG RYGGPGGGER ARGGGAGGAG GPGPGGLQPG QRVLYKQSIA QRARTMALYN PIPVKQNCFT VNRSLFVFSE DNVVRKYAK RITEWPPFEY MILATIIANC IVLALEQHLP DGDKTPMSER LDDTEPYFIG IFCFEAGIKI IALGFVFHKG S YLRNGWNV MDFVVVLTGI LATAGTDFDL RTLRAVRVLR PLKLVSGIPS LQVVLKSIMK AMVPLLQIGL LLFFAILMFA II GLEFYMG KFHKACFPNS TDAEPVGDFP CGKEAPARLC EGDTECREYW PGPNFGITNF DNILFAILTV FQCITMEGWT DIL YNTNDA AGNTWNWLYF IPLIIIGSFF MLNLVLGVLS GEFAKERERV ENRRAFLKLR RQQQIERELN GYLEWIFKAE EVML AEEDR NAEEKSPLDV LKRAATKKSR NDLIHAEEGE DRFADLCAVG SPFARASLKS GKTESSSYFR RKEKMFRFFI RRMVK AQSF YWVVLCVVAL NTLCVAMVHY NQPRRLTTTL YFAEFVFLGL FLTEMSLKMY GLGPRSYFRS SFNCFDFGVI VGSVFE VVW AAIKPGSSFG ISVLRALRLL RIFKVTKYWS SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFQDE TP TTNFDTFPAA ILTVFQILTG EDWNAVMYHG IESQGGVSKG MFSSFYFIVL TLFGNYTLLN VFLAIAVDNL ANAQELTK D EEEMEEAANQ KLALQKAKEV AEVSPMSAAN ISIAARQQNS AKARSVWEQR ASQLRLQNLR ASCEALYSEM DPEERLRFA TTRHLRPDMK THLDRPLVVE LGRDGARGPV GGKARPEAAE APEGVDPPRR HHRHRDKDKT PAAGDQDRAE APKAESGEPG AREERPRPH RSHSKEAAGP PEARSERGRG PGPEGGRRHH RRGSPEEAAE REPRRHRAHR HQDPSKECAG AKGERRARHR G GPRAGPRE AESGEEPARR HRARHKAQPA HEAVEKETTE KEATEKEAEI VEADKEKELR NHQPREPHCD LETSGTVTVG PM HTLPSTC LQKVEEQPED ADNQRNVTRM GSQPPDPNTI VHIPVMLTGP LGEATVVPSG NVDLESQAEG KKEVEADDVM RSG PRPIVP YSSMFCLSPT NLLRRFCHYI VTMRYFEVVI LVVIALSSIA LAAEDPVRTD SPRNNALKYL DYIFTGVFTF EMVI KMIDL GLLLHPGAYF RDLWNILDFI VVSGALVAFA FSGSKGKDIN TIKSLRVLRV LRPLKTIKRL PKLKAVFDCV VNSLK NVLN ILIVYMLFMF IFAVIAVQLF KGKFFYCTDE SKELERDCRG QYLDYEKEEV EAQPRQWKKY DFHYDNVLWA LLTLFT VST GEGWPMVLKH SVDATYEEQG PSPGYRMELS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKVMSECSLE KNERACI DF AISAKPLTRY MPQNRQSFQY KTWTFVVSPP FEYFIMAMIA LNTVVLMMKF YDAPYEYELM LKCLNIVFTS MFSMECVL K IIAFGVLNYF RDAWNVFDFV TVLGSITDIL VTEIAETNNF INLSFLRLFR AARLIKLLRQ GYTIRILLWT FVQSFKALP YVCLLIAMLF FIYAIIGMQV FGNIALDDDT SINRHNNFRT FLQALMLLFR SATGEAWHEI MLSCLSNQAC DEQANATECG SDFAYFYFV SFIFLCSFLM LNLFVAVIMD NFEYLTRDSS ILGPHHLDEF IRVWAEYDPA ACGRISYNDM FEMLKHMSPP L GLGKKCPA RVAYKRLVRM NMPISNEDMT VHFTSTLMAL IRTALEIKLA PAGTKQHQCD AELRKEISVV WANLPQKTLD LL VPPHKPD EMTVGKVYAA LMIFDFYKQN KTTRDQMQQA PGGLSQMGPV SLFHPLKATL EQTQPAVLRG ARVFLRQKSS TSL SNGGAI QNQESGIKES VSWGTQRTQD APHEARPPLE RGHSTEIPVG RSGALAVDVQ MQSITRRGPD GEPQPGLESQ GRAA SMPRL AAETQPVTDA SPMKRSISTL AQRPRGTHLC STTPDRPPPS QASSHHHHHR CHRRRDRKQR SLEKGPSLSA DMDGA PSSA VGPGLPPGEG PTGCRRERER RQERGRSQER RQPSSSSSEK QRFYSCDRFG GREPPKPKPS LSSHPTSPTA GQEPGP HPQ GSGSVNGSPL LSTSGASTPG RGGRRQLPQT PLTPRPSITY KTANSSPIHF AGAQTSLPAF SPGRLSRGLS EHNALLQ RD PLSQPLAPGS RIGSDPYLGQ RLDSEASVHA LPEDTLTFEE AVATNSGRSS RTSYVSSLTS QSHPLRRVPN GYHCTLGL S SGGRARHSYH HPDQDHWC

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Macromolecule #2: Voltage-dependent L-type calcium channel subunit beta-3

MacromoleculeName: Voltage-dependent L-type calcium channel subunit beta-3
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 54.607852 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MYDDSYVPGF EDSEAGSADS YTSRPSLDSD VSLEEDRESA RREVESQAQQ QLERAKHKPV AFAVRTNVSY CGVLDEECPV QGSGVNFEA KDFLHIKEKY SNDWWIGRLV KEGGDIAFIP SPQRLESIRL KQEQKARRSG NPSSLSDIGN RRSPPPSLAK Q KQKQAEHV ...String:
MYDDSYVPGF EDSEAGSADS YTSRPSLDSD VSLEEDRESA RREVESQAQQ QLERAKHKPV AFAVRTNVSY CGVLDEECPV QGSGVNFEA KDFLHIKEKY SNDWWIGRLV KEGGDIAFIP SPQRLESIRL KQEQKARRSG NPSSLSDIGN RRSPPPSLAK Q KQKQAEHV PPYDVVPSMR PVVLVGPSLK GYEVTDMMQK ALFDFLKHRF DGRISITRVT ADLSLAKRSV LNNPGKRTII ER SSARSSI AEVQSEIERI FELAKSLQLV VLDADTINHP AQLAKTSLAP IIVFVKVSSP KVLQRLIRSR GKSQMKHLTV QMM AYDKLV QCPPESFDVI LDENQLEDAC EHLAEYLEVY WRATHHPAPG PGLLGPPSAI PGLQNQQLLG ERGEEHSPLE RDSL MPSDE ASESSRQAWT GSSQRSSRHL EEDYADAYQD LYQPHRQHTS GLPSANGHDP QDRLLAQDSE HNHSDRNWQR NRPWP KDSY

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Macromolecule #3: Voltage-dependent calcium channel subunit alpha-2/delta-1

MacromoleculeName: Voltage-dependent calcium channel subunit alpha-2/delta-1
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 124.692469 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAAGCLLALT LTLFQSLLIG PSSEEPFPSA VTIKSWVDKM QEDLVTLAKT ASGVNQLVDI YEKYQDLYTV EPNNARQLVE IAARDIEKL LSNRSKALVR LALEAEKVQA AHQWREDFAS NEVVYYNAKD DLDPEKNDSE PGSQRIKPVF IEDANFGRQI S YQHAAVHI ...String:
MAAGCLLALT LTLFQSLLIG PSSEEPFPSA VTIKSWVDKM QEDLVTLAKT ASGVNQLVDI YEKYQDLYTV EPNNARQLVE IAARDIEKL LSNRSKALVR LALEAEKVQA AHQWREDFAS NEVVYYNAKD DLDPEKNDSE PGSQRIKPVF IEDANFGRQI S YQHAAVHI PTDIYEGSTI VLNELNWTSA LDEVFKKNRE EDPSLLWQVF GSATGLARYY PASPWVDNSR TPNKIDLYDV RR RPWYIQG AASPKDMLIL VDVSGSVSGL TLKLIRTSVS EMLETLSDDD FVNVASFNSN AQDVSCFQHL VQANVRNKKV LKD AVNNIT AKGITDYKKG FSFAFEQLLN YNVSRANCNK IIMLFTDGGE ERAQEIFNKY NKDKKVRVFT FSVGQHNYDR GPIQ WMACE NKGYYYEIPS IGAIRINTQE YLDVLGRPMV LAGDKAKQVQ WTNVYLDALE LGLVITGTLP VFNITGQFEN KTNLK NQLI LGVMGVDVSL EDIKRLTPRF TLCPNGYYFA IDPNGYVLLH PNLQPKPIGV GIPTINLRKR RPNIQNPKSQ EPVTLD FLD AELENDIKVE IRNKMIDGES GEKTFRTLVK SQDERYIDKG NRTYTWTPVN GTDYSLALVL PTYSFYYIKA KLEETIT QA RYSETLKPDN FEESGYTFIA PRDYCNDLKI SDNNTEFLLN FNEFIDRKTP NNPSCNADLI NRVLLDAGFT NELVQNYW S KQKNIKGVKA RFVVTDGGIT RVYPKEAGEN WQENPETYED SFYKRSLDND NYVFTAPYFN KSGPGAYESG IMVSKAVEI YIQGKLLKPA VVGIKIDVNS WIENFTKTSI RDPCAGPVCD CKRNSDVMDC VILDDGGFLL MANHDDYTNQ IGRFFGEIDP SLMRHLVNI SVYAFNKSYD YQSVCEPGAA PKQGAGHRSA YVPSVADILQ IGWWATAAAW SILQQFLLSL TFPRLLEAVE M EDDDFTAS LSKQSCITEQ TQYFFDNDSK SFSGVLDCGN CSRIFHGEKL MNTNLIFIMV ESKGTCPCDT RLLIQAEQTS DG PNPCDMV KQPRYRKGPD VCFDNNVLED YTDCGGVSGL NPSLWYIIGI QFLLLWLVSG STHRLL

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Macromolecule #7: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 7 / Number of copies: 3 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

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Macromolecule #8: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 8 / Number of copies: 2 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #9: CHOLESTEROL HEMISUCCINATE

MacromoleculeName: CHOLESTEROL HEMISUCCINATE / type: ligand / ID: 9 / Number of copies: 3 / Formula: Y01
Molecular weightTheoretical: 486.726 Da
Chemical component information

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

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Macromolecule #10: CHOLESTEROL

MacromoleculeName: CHOLESTEROL / type: ligand / ID: 10 / Number of copies: 4 / Formula: CLR
Molecular weightTheoretical: 386.654 Da
Chemical component information

ChemComp-CLR:
CHOLESTEROL / Cholesterol

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Macromolecule #11: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 11 / Number of copies: 2 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

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Macromolecule #12: [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tr...

MacromoleculeName: [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate
type: ligand / ID: 12 / Number of copies: 1 / Formula: PT5
Molecular weightTheoretical: 1.047088 KDa

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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

Concentration20 mg/mL
BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV / Details: blot for 6 seconds before plunging.
DetailsCav2.2

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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
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 56615

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