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- EMDB-43908: Structure of human calcium-sensing receptor in complex with Gi3 p... -

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Basic information

Entry
Database: EMDB / ID: EMD-43908
TitleStructure of human calcium-sensing receptor in complex with Gi3 protein in nanodiscs
Map dataHuman CaSR-Gi3 complex in nanodiscs, composite map of locally refined CaSR ECD, CaSR TMD and G protein.
Sample
  • Complex: Human CaSR in complex with Gi3 protein
    • Protein or peptide: x 4 types
  • Ligand: x 7 types
KeywordsCalcium-sensing receptor / G-protein-coupled receptor / G protein / signal transduction / MEMBRANE PROTEIN
Function / homology
Function and homology information


regulation of presynaptic membrane potential / bile acid secretion / chemosensory behavior / response to fibroblast growth factor / cellular response to peptide / cellular response to vitamin D / phosphatidylinositol-4,5-bisphosphate phospholipase C activity / negative regulation of adenylate cyclase activity / Class C/3 (Metabotropic glutamate/pheromone receptors) / calcium ion import ...regulation of presynaptic membrane potential / bile acid secretion / chemosensory behavior / response to fibroblast growth factor / cellular response to peptide / cellular response to vitamin D / phosphatidylinositol-4,5-bisphosphate phospholipase C activity / negative regulation of adenylate cyclase activity / Class C/3 (Metabotropic glutamate/pheromone receptors) / calcium ion import / regulation of potassium ion transmembrane transport / GTP metabolic process / positive regulation of positive chemotaxis / fat pad development / cellular response to hepatocyte growth factor stimulus / amino acid binding / branching morphogenesis of an epithelial tube / positive regulation of calcium ion import / positive regulation of vasoconstriction / regulation of calcium ion transport / positive regulation of macroautophagy / cellular response to low-density lipoprotein particle stimulus / anatomical structure morphogenesis / detection of calcium ion / Adenylate cyclase inhibitory pathway / JNK cascade / axon terminus / ossification / chloride transmembrane transport / response to ischemia / cellular response to glucose stimulus / G protein-coupled receptor binding / G protein-coupled receptor activity / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / positive regulation of insulin secretion / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / G-protein beta/gamma-subunit complex binding / centriolar satellite / vasodilation / integrin binding / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / G-protein activation / intracellular calcium ion homeostasis / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / Glucagon signaling in metabolic regulation / G beta:gamma signalling through BTK / ADP signalling through P2Y purinoceptor 12 / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / Vasopressin regulates renal water homeostasis via Aquaporins / GDP binding / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / G alpha (z) signalling events / cellular response to catecholamine stimulus / ADP signalling through P2Y purinoceptor 1 / ADORA2B mediated anti-inflammatory cytokines production / G beta:gamma signalling through PI3Kgamma / adenylate cyclase-activating dopamine receptor signaling pathway / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / cellular response to prostaglandin E stimulus / G-protein beta-subunit binding / heterotrimeric G-protein complex / G alpha (12/13) signalling events / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / presynaptic membrane / GTPase binding / Ca2+ pathway / fibroblast proliferation / midbody / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / G alpha (i) signalling events / G alpha (s) signalling events / phospholipase C-activating G protein-coupled receptor signaling pathway / basolateral plasma membrane / G alpha (q) signalling events / cellular response to hypoxia / vesicle / transmembrane transporter binding / Extra-nuclear estrogen signaling / positive regulation of ERK1 and ERK2 cascade / ciliary basal body / apical plasma membrane / G protein-coupled receptor signaling pathway / lysosomal membrane / cell division / focal adhesion / neuronal cell body / GTPase activity / positive regulation of cell population proliferation / calcium ion binding / synapse / centrosome / positive regulation of gene expression
Similarity search - Function
GPCR, family 3, extracellular calcium-sensing receptor-related / G-protein coupled receptors family 3 signature 1. / G-protein coupled receptors family 3 signature 3. / G-protein coupled receptors family 3 signature 2. / GPCR, family 3, nine cysteines domain / GPCR, family 3, nine cysteines domain superfamily / Nine Cysteines Domain of family 3 GPCR / GPCR, family 3, conserved site / GPCR, family 3 / G-protein coupled receptors family 3 profile. ...GPCR, family 3, extracellular calcium-sensing receptor-related / G-protein coupled receptors family 3 signature 1. / G-protein coupled receptors family 3 signature 3. / G-protein coupled receptors family 3 signature 2. / GPCR, family 3, nine cysteines domain / GPCR, family 3, nine cysteines domain superfamily / Nine Cysteines Domain of family 3 GPCR / GPCR, family 3, conserved site / GPCR, family 3 / G-protein coupled receptors family 3 profile. / GPCR family 3, C-terminal / 7 transmembrane sweet-taste receptor of 3 GCPR / G-protein alpha subunit, group I / Receptor, ligand binding region / Receptor family ligand binding region / Periplasmic binding protein-like I / Guanine nucleotide binding protein (G-protein), alpha subunit / G protein alpha subunit, helical insertion / G-protein alpha subunit / G-alpha domain profile. / G protein alpha subunit / G-protein, gamma subunit / G-protein gamma subunit domain profile. / G-protein gamma-like domain / G-protein gamma-like domain superfamily / GGL domain / G protein gamma subunit-like motifs / GGL domain / G protein beta WD-40 repeat protein / Guanine nucleotide-binding protein, beta subunit / G-protein, beta subunit / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Guanine nucleotide-binding protein G(i) subunit alpha-3 / Extracellular calcium-sensing receptor / Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 / Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsZuo H / Park J / Frangaj A / Ye J / Lu G / Manning JJ / Asher WB / Lu Z / Hu G / Wang L ...Zuo H / Park J / Frangaj A / Ye J / Lu G / Manning JJ / Asher WB / Lu Z / Hu G / Wang L / Mendez J / Eng E / Zhang Z / Lin X / Grasucci R / Hendrickson WA / Clarke OB / Javitch JA / Conigrave AD / Fan QR
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM141871 United States
CitationJournal: Nature / Year: 2024
Title: Promiscuous G-protein activation by the calcium-sensing receptor.
Authors: Hao Zuo / Jinseo Park / Aurel Frangaj / Jianxiang Ye / Guanqi Lu / Jamie J Manning / Wesley B Asher / Zhengyuan Lu / Guo-Bin Hu / Liguo Wang / Joshua Mendez / Edward Eng / Zhening Zhang / ...Authors: Hao Zuo / Jinseo Park / Aurel Frangaj / Jianxiang Ye / Guanqi Lu / Jamie J Manning / Wesley B Asher / Zhengyuan Lu / Guo-Bin Hu / Liguo Wang / Joshua Mendez / Edward Eng / Zhening Zhang / Xin Lin / Robert Grassucci / Wayne A Hendrickson / Oliver B Clarke / Jonathan A Javitch / Arthur D Conigrave / Qing R Fan /
Abstract: The human calcium-sensing receptor (CaSR) detects fluctuations in the extracellular Ca concentration and maintains Ca homeostasis. It also mediates diverse cellular processes not associated with Ca ...The human calcium-sensing receptor (CaSR) detects fluctuations in the extracellular Ca concentration and maintains Ca homeostasis. It also mediates diverse cellular processes not associated with Ca balance. The functional pleiotropy of CaSR arises in part from its ability to signal through several G-protein subtypes. We determined structures of CaSR in complex with G proteins from three different subfamilies: G, G and G. We found that the homodimeric CaSR of each complex couples to a single G protein through a common mode. This involves the C-terminal helix of each Gα subunit binding to a shallow pocket that is formed in one CaSR subunit by all three intracellular loops (ICL1-ICL3), an extended transmembrane helix 3 and an ordered C-terminal region. G-protein binding expands the transmembrane dimer interface, which is further stabilized by phospholipid. The restraint imposed by the receptor dimer, in combination with ICL2, enables G-protein activation by facilitating conformational transition of Gα. We identified a single Gα residue that determines G and G versus G selectivity. The length and flexibility of ICL2 allows CaSR to bind all three Gα subtypes, thereby conferring capacity for promiscuous G-protein coupling.
History
DepositionMar 4, 2024-
Header (metadata) releaseApr 17, 2024-
Map releaseApr 17, 2024-
UpdateNov 20, 2024-
Current statusNov 20, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_43908.png

Downloads & links

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Map

FileDownload / File: emd_43908.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationHuman CaSR-Gi3 complex in nanodiscs, composite map of locally refined CaSR ECD, CaSR TMD and G protein.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 512 pix.
= 432.128 Å		0.84 Å/pix.
x 512 pix.
= 432.128 Å		0.84 Å/pix.
x 512 pix.
= 432.128 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.844 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.3
Minimum - Maximum0.0 - 4.3243546
Average (Standard dev.)0.0019188453 (±0.04067776)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 432.128 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Human CaSR in complex with Gi3 protein

EntireName: Human CaSR in complex with Gi3 protein
Components
  • Complex: Human CaSR in complex with Gi3 protein
    • Protein or peptide: Isoform 1 of Extracellular calcium-sensing receptor
    • Protein or peptide: Guanine nucleotide-binding protein G(i) subunit alpha-3
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: CYCLOMETHYLTRYPTOPHAN
  • Ligand: PHOSPHATE ION
  • Ligand: CALCIUM ION
  • Ligand: 3-(2-chlorophenyl)-N-[(1R)-1-(3-methoxyphenyl)ethyl]propan-1-amine
  • Ligand: CHOLESTEROL HEMISUCCINATE
  • Ligand: (19R,22S,25R)-22,25,26-trihydroxy-16,22-dioxo-17,21,23-trioxa-22lambda~5~-phosphahexacosan-19-yl (9Z)-octadec-9-enoate

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Supramolecule #1: Human CaSR in complex with Gi3 protein

SupramoleculeName: Human CaSR in complex with Gi3 protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 288 KDa

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Macromolecule #1: Isoform 1 of Extracellular calcium-sensing receptor

MacromoleculeName: Isoform 1 of Extracellular calcium-sensing receptor / type: protein_or_peptide / ID: 1
Details: The CaSR construct consists of residues 1-903 and a Flag tag inserted after the signal peptide.
Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 102.864617 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAFYSCCWVL LALTWHTSAD YKDDDDKYGP DQRAQKKGDI ILGGLFPIHF GVAAKDQDLK SRPESVECIR YNFRGFRWLQ AMIFAIEEI NSSPALLPNL TLGYRIFDTC NTVSKALEAT LSFVAQNKID SLNLDEFCNC SEHIPSTIAV VGATGSGVST A VANLLGLF ...String:
MAFYSCCWVL LALTWHTSAD YKDDDDKYGP DQRAQKKGDI ILGGLFPIHF GVAAKDQDLK SRPESVECIR YNFRGFRWLQ AMIFAIEEI NSSPALLPNL TLGYRIFDTC NTVSKALEAT LSFVAQNKID SLNLDEFCNC SEHIPSTIAV VGATGSGVST A VANLLGLF YIPQVSYASS SRLLSNKNQF KSFLRTIPND EHQATAMADI IEYFRWNWVG TIAADDDYGR PGIEKFREEA EE RDICIDF SELISQYSDE EEIQHVVEVI QNSTAKVIVV FSSGPDLEPL IKEIVRRNIT GKIWLASEAW ASSSLIAMPQ YFH VVGGTI GFALKAGQIP GFREFLKKVH PRKSVHNGFA KEFWEETFNC HLQEGAKGPL PVDTFLRGHE ESGDRFSNSS TAFR PLCTG DENISSVETP YIDYTHLRIS YNVYLAVYSI AHALQDIYTC LPGRGLFTNG SCADIKKVEA WQVLKHLRHL NFTNN MGEQ VTFDECGDLV GNYSIINWHL SPEDGSIVFK EVGYYNVYAK KGERLFINEE KILWSGFSRE VPFSNCSRDC LAGTRK GII EGEPTCCFEC VECPDGEYSD ETDASACNKC PDDFWSNENH TSCIAKEIEF LSWTEPFGIA LTLFAVLGIF LTAFVLG VF IKFRNTPIVK ATNRELSYLL LFSLLCCFSS SLFFIGEPQD WTCRLRQPAF GISFVLCISC ILVKTNRVLL VFEAKIPT S FHRKWWGLNL QFLLVFLCTF MQIVICVIWL YTAPPSSYRN QELEDEIIFI TCHEGSLMAL GFLIGYTCLL AAICFFFAF KSRKLPENFN EAKFITFSML IFFIVWISFI PAYASTYGKF VSAVEVIAIL AASFGLLACI FFNKIYIILF KPSRNTIEEV RCSTAAHAF KVAARATLRR SNVSRKRSSS LG

UniProtKB: Extracellular calcium-sensing receptor

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Macromolecule #2: Guanine nucleotide-binding protein G(i) subunit alpha-3

MacromoleculeName: Guanine nucleotide-binding protein G(i) subunit alpha-3
type: protein_or_peptide / ID: 2
Details: G(i3)alpha contains four dominant negative mutations, S47N, G203A, E245A, and A326S
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 40.584156 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKNTIV KQMKIIHEDG YSEDECKQYK VVVYSNTIQS IIAIIRAMG RLKIDFGEAA RADDARQLFV LAGSAEEGVM TPELAGVIKR LWRDGGVQAC FSRSREYQLN DSASYYLNDL D RISQSNYI ...String:
MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKNTIV KQMKIIHEDG YSEDECKQYK VVVYSNTIQS IIAIIRAMG RLKIDFGEAA RADDARQLFV LAGSAEEGVM TPELAGVIKR LWRDGGVQAC FSRSREYQLN DSASYYLNDL D RISQSNYI PTQQDVLRTR VKTTGIVETH FTFKDLYFKM FDVGAQRSER KKWIHCFEGV TAIIFCVALS DYDLVLAEDE EM NRMHASM KLFDSICNNK WFTETSIILF LNKKDLFEEK IKRSPLTICY PEYTGSNTYE EAAAYIQCQF EDLNRRKDTK EIY THFTCS TDTKNVQFVF DAVTDVIIKN NLKECGLY

UniProtKB: Guanine nucleotide-binding protein G(i) subunit alpha-3

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Macromolecule #3: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2

MacromoleculeName: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
type: protein_or_peptide / ID: 3
Details: GNB2 has N-terminal Flag tag inserted after the initial Met.
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 38.367969 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MDYKDDDDKS ELEQLRQEAE QLRNQIRDAR KACGDSTLTQ ITAGLDPVGR IQMRTRRTLR GHLAKIYAMH WGTDSRLLVS ASQDGKLII WDSYTTNKVH AIPLRSSWVM TCAYAPSGNF VACGGLDNIC SIYSLKTREG NVRVSRELPG HTGYLSCCRF L DDNQIITS ...String:
MDYKDDDDKS ELEQLRQEAE QLRNQIRDAR KACGDSTLTQ ITAGLDPVGR IQMRTRRTLR GHLAKIYAMH WGTDSRLLVS ASQDGKLII WDSYTTNKVH AIPLRSSWVM TCAYAPSGNF VACGGLDNIC SIYSLKTREG NVRVSRELPG HTGYLSCCRF L DDNQIITS SGDTTCALWD IETGQQTVGF AGHSGDVMSL SLAPDGRTFV SGACDASIKL WDVRDSMCRQ TFIGHESDIN AV AFFPNGY AFTTGSDDAT CRLFDLRADQ ELLMYSHDNI ICGITSVAFS RSGRLLLAGY DDFNCNIWDA MKGDRAGVLA GHD NRVSCL GVTDDGMAVA TGSWDSFLKI WN

UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2

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Macromolecule #4: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

MacromoleculeName: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.861143 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP FREKKFFCAI L

UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

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Macromolecule #6: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 6 / Number of copies: 4 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Macromolecule #7: CYCLOMETHYLTRYPTOPHAN

MacromoleculeName: CYCLOMETHYLTRYPTOPHAN / type: ligand / ID: 7 / Number of copies: 2 / Formula: TCR
Molecular weightTheoretical: 216.236 Da
Chemical component information

ChemComp-TCR:
CYCLOMETHYLTRYPTOPHAN

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Macromolecule #8: PHOSPHATE ION

MacromoleculeName: PHOSPHATE ION / type: ligand / ID: 8 / Number of copies: 2 / Formula: PO4
Molecular weightTheoretical: 94.971 Da
Chemical component information

ChemComp-PO4:
PHOSPHATE ION

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Macromolecule #9: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 9 / Number of copies: 6 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #10: 3-(2-chlorophenyl)-N-[(1R)-1-(3-methoxyphenyl)ethyl]propan-1-amine

MacromoleculeName: 3-(2-chlorophenyl)-N-[(1R)-1-(3-methoxyphenyl)ethyl]propan-1-amine
type: ligand / ID: 10 / Number of copies: 2 / Formula: 9IG
Molecular weightTheoretical: 303.826 Da
Chemical component information

ChemComp-9IG:
3-(2-chlorophenyl)-N-[(1R)-1-(3-methoxyphenyl)ethyl]propan-1-amine

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Macromolecule #11: CHOLESTEROL HEMISUCCINATE

MacromoleculeName: CHOLESTEROL HEMISUCCINATE / type: ligand / ID: 11 / Number of copies: 1 / Formula: Y01
Molecular weightTheoretical: 486.726 Da
Chemical component information

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

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Macromolecule #12: (19R,22S,25R)-22,25,26-trihydroxy-16,22-dioxo-17,21,23-trioxa-22l...

MacromoleculeName: (19R,22S,25R)-22,25,26-trihydroxy-16,22-dioxo-17,21,23-trioxa-22lambda~5~-phosphahexacosan-19-yl (9Z)-octadec-9-enoate
type: ligand / ID: 12 / Number of copies: 1 / Formula: A1AF7
Molecular weightTheoretical: 749.007 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

Concentration3.5 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4SHEPES
100.0 mMNaClSodium chloride
2.0 mMMgCl2Magnesium chloride
10.0 mMCaCl2Calcium chloride
20.0 uMC12H12N2O2TNCA
20.0 uMC18H22ClNOHClR568 HCl
GridModel: Quantifoil R0.6/1 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Support film - Film thickness: 50 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 25 sec. / Pretreatment - Atmosphere: OTHER
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
Details: The sample was blotted for 6s before plunge-frozen..

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Electron microscopy

MicroscopeFEI TITAN KRIOS
TemperatureMax: 100.0 K
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
SoftwareName: Leginon (ver. 3.6)
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 2 / Number real images: 16504 / Average exposure time: 2.5 sec. / Average electron dose: 70.14 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: 1.8 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000
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

Particle selectionNumber selected: 2792317
Startup modelType of model: OTHER / Details: Ab initio
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.3.2) / Number images used: 55985
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.3.2)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.3.2)

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Atomic model buiding 1

Initial model
PDB IDChain

7sil

chain_id: Q, source_name: PDB, initial_model_type: experimental model

7sil

chain_id: R, source_name: PDB, initial_model_type: experimental model

7s8m

chain_id: A, source_name: PDB, initial_model_type: experimental model

7s8m

chain_id: B, source_name: PDB, initial_model_type: experimental model

7s8m

chain_id: G, source_name: PDB, initial_model_type: experimental model
SoftwareName: Coot (ver. 0.9.8.1)
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9avl:
Structure of human calcium-sensing receptor in complex with Gi3 protein in nanodiscs

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