[English] 日本語
![](img/lk-miru.gif)
- EMDB-22016: Wt pig RyR1 in complex with apoCaM, EGTA condition (class 3, open) -
+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-22016 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Wt pig RyR1 in complex with apoCaM, EGTA condition (class 3, open) | |||||||||
![]() | RyR1, FKBP12.6, CaM | |||||||||
![]() |
| |||||||||
![]() | receptor / calcium / channel / complex / TRANSPORT PROTEIN-ISOMERASE-CALCIUM BINDING PROTEIN complex | |||||||||
Function / homology | ![]() positive regulation of sequestering of calcium ion / cyclic nucleotide binding / negative regulation of insulin secretion involved in cellular response to glucose stimulus / negative regulation of release of sequestered calcium ion into cytosol / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / cell communication by electrical coupling involved in cardiac conduction ...positive regulation of sequestering of calcium ion / cyclic nucleotide binding / negative regulation of insulin secretion involved in cellular response to glucose stimulus / negative regulation of release of sequestered calcium ion into cytosol / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / cell communication by electrical coupling involved in cardiac conduction / Calmodulin induced events / response to redox state / protein maturation by protein folding / Reduction of cytosolic Ca++ levels / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of Ca-permeable Kainate Receptor / 'de novo' protein folding / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / negative regulation of high voltage-gated calcium channel activity / CaMK IV-mediated phosphorylation of CREB / positive regulation of cyclic-nucleotide phosphodiesterase activity / Glycogen breakdown (glycogenolysis) / negative regulation of heart rate / organelle localization by membrane tethering / negative regulation of calcium ion export across plasma membrane / CLEC7A (Dectin-1) induces NFAT activation / regulation of cardiac muscle cell action potential / autophagosome membrane docking / mitochondrion-endoplasmic reticulum membrane tethering / negative regulation of phosphoprotein phosphatase activity / Activation of RAC1 downstream of NMDARs / FK506 binding / positive regulation of ryanodine-sensitive calcium-release channel activity / regulation of cell communication by electrical coupling involved in cardiac conduction / positive regulation of axon regeneration / Negative regulation of NMDA receptor-mediated neuronal transmission / negative regulation of peptidyl-threonine phosphorylation / Synthesis of IP3 and IP4 in the cytosol / Unblocking of NMDA receptors, glutamate binding and activation / Phase 0 - rapid depolarisation / protein phosphatase activator activity / RHO GTPases activate PAKs / positive regulation of phosphoprotein phosphatase activity / Ion transport by P-type ATPases / Long-term potentiation / Uptake and function of anthrax toxins / : / Regulation of MECP2 expression and activity / Calcineurin activates NFAT / catalytic complex / DARPP-32 events / detection of calcium ion / smooth muscle contraction / regulation of cardiac muscle contraction / negative regulation of ryanodine-sensitive calcium-release channel activity / Smooth Muscle Contraction / response to vitamin E / calcium channel inhibitor activity / RHO GTPases activate IQGAPs / cellular response to interferon-beta / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / Protein methylation / protein peptidyl-prolyl isomerization / eNOS activation / Activation of AMPK downstream of NMDARs / T cell proliferation / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / release of sequestered calcium ion into cytosol / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / positive regulation of protein dephosphorylation / regulation of calcium-mediated signaling / Ion homeostasis / titin binding / regulation of ryanodine-sensitive calcium-release channel activity / voltage-gated potassium channel complex / positive regulation of protein autophosphorylation / sperm midpiece / sarcoplasmic reticulum membrane / calcium channel complex / regulation of cytosolic calcium ion concentration / substantia nigra development / adenylate cyclase activator activity / Ras activation upon Ca2+ influx through NMDA receptor / regulation of heart rate / sarcomere / protein serine/threonine kinase activator activity / FCERI mediated Ca+2 mobilization / FCGR3A-mediated IL10 synthesis / VEGFR2 mediated vascular permeability / positive regulation of peptidyl-threonine phosphorylation / regulation of cytokinesis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / VEGFR2 mediated cell proliferation / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RAF activation / positive regulation of receptor signaling pathway via JAK-STAT Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||
![]() | Woll KW / Haji-Ghassemi O | |||||||||
Funding support | 1 items
| |||||||||
![]() | ![]() Title: Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM. Authors: Kellie A Woll / Omid Haji-Ghassemi / Filip Van Petegem / ![]() Abstract: Ryanodine Receptors (RyRs) are massive channels that release Ca from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to malignant hyperthermia (MH), myopathies, and ...Ryanodine Receptors (RyRs) are massive channels that release Ca from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to malignant hyperthermia (MH), myopathies, and arrhythmias. Here, we explore the first MH mutation identified in humans by providing cryo-EM snapshots of the pig homolog, R615C, showing that it affects an interface between three solenoid regions. We also show the impact of apo-calmodulin (apoCaM) and how it can induce opening by bending of the bridging solenoid, mediated by its N-terminal lobe. For R615C RyR1, apoCaM binding abolishes a pathological 'intermediate' conformation, distributing the population to a mixture of open and closed channels, both different from the structure without apoCaM. Comparisons show that the mutation primarily affects the closed state, inducing partial movements linked to channel activation. This shows that disease mutations can cause distinct pathological conformations of the RyR and facilitate channel opening by disrupting interactions between different solenoid regions. | |||||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-EMDB archive
Map data | ![]() | 57.4 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 18.6 KB 18.6 KB | Display Display | ![]() |
Images | ![]() | 209.7 KB | ||
Filedesc metadata | ![]() | 7.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 457.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 457 KB | Display | |
Data in XML | ![]() | 7.7 KB | Display | |
Data in CIF | ![]() | 8.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6x33MC ![]() 6w1nC ![]() 6x32C ![]() 6x34C ![]() 6x35C ![]() 6x36C C: citing same article ( M: atomic model generated by this map |
---|---|
Similar structure data |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | RyR1, FKBP12.6, CaM | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.09 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-
Sample components
-Entire : ryanodine receptor-FKBP1B-Calmodulin complex
Entire | Name: ryanodine receptor-FKBP1B-Calmodulin complex |
---|---|
Components |
|
-Supramolecule #1: ryanodine receptor-FKBP1B-Calmodulin complex
Supramolecule | Name: ryanodine receptor-FKBP1B-Calmodulin complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
---|
-Supramolecule #2: ryanodine receptor
Supramolecule | Name: ryanodine receptor / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2 |
---|---|
Source (natural) | Organism: ![]() ![]() |
-Supramolecule #3: FKBP1B
Supramolecule | Name: FKBP1B / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1 |
---|---|
Source (natural) | Organism: ![]() |
-Supramolecule #4: Calmodulin
Supramolecule | Name: Calmodulin / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3 |
---|---|
Source (natural) | Organism: ![]() |
-Macromolecule #1: Peptidyl-prolyl cis-trans isomerase FKBP1B
Macromolecule | Name: Peptidyl-prolyl cis-trans isomerase FKBP1B / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 11.667305 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GVEIETISPG DGRTFPKKGQ TCVVHYTGML QNGKKFDSSR DRNKPFKFRI GKQEVIKGFE EGAAQMSLGQ RAKLTCTPDV AYGATGHPG VIPPNATLIF DVELLNLE UniProtKB: Peptidyl-prolyl cis-trans isomerase FKBP1B |
-Macromolecule #2: Ryanodine Receptor
Macromolecule | Name: Ryanodine Receptor / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 425.09225 KDa |
Sequence | String: QFLRTDDEVV LQCNATVLKE QLKLCLAAEG FGNRLCFLEP TSNAQNVPPD LAICCFVLEQ SLSVRALQEM LANGHRTLLY GHAILLRHA HSGMYLSCLT TSRSMTDKLA FDVGLQEDAT GEACWWTTHP ASKQRSEGEK VRVGDDLILV SVSSERYLHL S TASGELQV ...String: QFLRTDDEVV LQCNATVLKE QLKLCLAAEG FGNRLCFLEP TSNAQNVPPD LAICCFVLEQ SLSVRALQEM LANGHRTLLY GHAILLRHA HSGMYLSCLT TSRSMTDKLA FDVGLQEDAT GEACWWTTHP ASKQRSEGEK VRVGDDLILV SVSSERYLHL S TASGELQV DASFMQTLWN MNPICSGCEE GYVTGGHVLR LFHGHMDECL TISPADSDDQ RRLVYYEGGS VCTHARSLWR LE PLRISWS GSHLRWGQPL RIRHVTTGRY LALIEDQGLV VVDASKAHTK ATSFCFRISK EKLKRDVEGM GPPEIKYGES LCF VQHVAS GLWLTYAALK KKAILHQEGH MDDALSLTRC QQEESQAARM IYSTAGLYNH FIKGLDSFSG KPRGSGAPAG TALP LEGVI LSLQDLIGYF EPPSEELQHE EKQSKLRSLR NRQSLFQEEG MLSLVLNCID RLNVYTTAAH FAEFAGEEAA ESWKE IVNL LYEILASLIR GNRANCALFS NNLDWLVSKL DRLEASSGIL EVLYCVLIES PEVLNIIQEN HIKSIISLLD KHGRNH KVL DVLCSLCVCN GVAVRSNQDL ITENLLPGRE LLLQTNLINY VTSIRPNIFV GRAEGTTQYS KWYFEVMVDE VVPFLTA QA THLRVGWALT EGYSPYPGGG EGWGGNGVGD DLYSYGFDGL HLWTGHVPRL VTSPGQHLLA PEDVVSCCLD LSVPSISF R INGCPVQGVF EAFNLNGLFF PVVSFSAGVK VRFLLGGRHG EFKFLPPPGY APCHEAVLPR ERLRLEPIKE YRREGPRGP HLVGPSRCLS HTDFVPCHLE RIREKLAENI HELWALTRIE QGWTYGPVRD DNKRLHPCLV DFHSLPEPER NYNLQMSGET LKTLLALGC HVGMADEKAE DNLRKTKLPK TYMMSNGYKP APLDLSHVRL TPAQTTLVDR LAENGHNVWA RDRVAQGWSY S AVQDIPAR RNPRLVPYRL LDEATKRSNR DSLCQAVRTL LGYGYNIERV RIFRAEKSYA VQSGRWYFEF EAVTTGEMRV GW ARPELRP DVELGADELA YVFNGHRGQR WHLGSELFGR PWQSGDVVGC MIDLTENTII FTLNGEVLMS DSGSETAFRD IEV GDGFLP VCSLGPGQVG HLNLGQDVSS LRFFAICGLQ EGFEPFAINM QRPVTTWFSK SLPQFEAVPL EHPHYEVSRV DGTV DTPPC LRLTHRSLVE MLFLRLSLPV QFHQLNTTTY YYSVRVFAGQ EPSCVWVGWV TPDYHQHDMN FDLTKVRAVT VTMGD NIHS SLKCSNCYMV WGGDFVSHTD LVIGCLVDLA TGLMTFTANG KESNTFFQVE PNTKLFPAVF VLPTHQNVIQ FELGKQ KNI MPLSAAMFLS ERKNPAPQCP PRLEMQMLMP VSWSRMPNHF LRVETRRAGE RLGWAVQCQE PLTMMALHIP EENRCMD IL ELSERLDLQQ FHSHTLRLYR AVCALGNNRV AHALCSHVDQ AQLLHALEDA HLPGPLRAGY YDLLISIHLE SACRSRRS M LSEYIVPLTP ETRAITLFPP RHGLPGVGVT TSLRPPHHFS APCFVAALPE APARLSPSIP LEALRDKALR MLGEAVRDG GQHARDPVGG SVEFQFVPVL KLVSTLLVMG IFGDEDVKQI LKMIEPEVEE GLLQMKLPES VKLQMCNLLE YFCDQELQHR VESLAAFAE RYVDKLQANQ RDRYGILMKA FTMTAAETAR RTREFRSPPQ EQINMLLHFK PLPDEIRQDL LEFHQDLLTH C GIQLQSLQ ELVSHTVVRW AQEDFVQSPE LVRAMFSLLH RQYDGLGELL RALPRAYTIS PSSVEDTMSL LECLGQIRSL LI VQMGPQE ENLMIQSIGN IMNNKVFYQH PNLMRALGMH ETVMEVMVNV LRFPKMVTSC CRFLCYFCRI SRQNQRSMFD HLS YLLENS GGMQGSTPLD VAAASVIDNN ELALALQEQD LEKVVSYLAG CGLQSCPMLL AKGYPDIGWN PCGGERYLDF LRFA VFVNG ESVEENANVV VRLLIRKPEC FGPALRGEGG SGLLATIEEA IHLGHAIMSF YAALIDLLGR CAPEMHLIQA GKGEA LRIR AILRSLVPLD DLVGIISLPL QIPMSASFVP DHKASMVLFL DRVYGIENQD FLLHVLDVGF LPDMRAAALA LNRYLC LAV LPLITKCAPL FAMVDSMLHT VYRLSRGRSL TKAQRDVIEE CLMALCRYIR PSMLQHLLRR LVF(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)DPRPVETL NVIIPEKLDS FI NKFAEYT HEKWAFDKIQ NNWSYGENID EELKTHPMLR PYKTFSEKDK EIYRWPIKES LKAMIAWEWT IEKAREGEYN PQP PDLSGV TLSRELQAMA EQLAENYHNT WGRKKKQELE AKGGGTHPLL VPYDTLTAKE KARDREKAQE LLKFLQMNGY AVTR (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)F SVLCRDLYAL YPLL IRYVD NNRAHWLTEP NPSAEELFRM VGEIFIYWSK SHNFKREEQN FVV(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)HKLLS KQRRR AVVA CFRMTPLYNL PTHRACNMFL ESYKAAWILT EDHSFEDRMI DDLSKAGEQE EEEEEVEEKK PDPLHQLVLH FSRTAL TEK SKLDEDYLYM AYADIMAKSC HLEESFEEKE MEKQRLLYQQ ARLHNRGAAE MVLQMISACK GETGAMVSST LKLGISI LN GGNADVQQKM LDYLKDKKEV GFFQSIQALM QTCSVLDLNA FERQNKAEGL GMVNEDGTVI GEKVMADDEF TQDLFRFL Q LLCEGHNNDF QNYLRTQTGN TTTINIIICT VDYLLRLQES ISDFYWYYSG KDVIEEQGKR NFSKAMSVAK QVFNSLTEY IQGPCTGNQQ SLAHSRLWDA VVGFLHVFAH MMMKLAQDSS QIELLKELLD LQKDMVVMLL SLLEGNVVNG MIARQMVDML VESSSNVEM ILKFFDMFLK LKDIVGSEAF QDYVTDPRGL ISKKDFQK(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)EFA NR FQEPARDIGF NVAVLLTNLS EHVPHDPRLR NFLELAESIL EYFRPYLGRI EIMGASRRIE RIYFEISETN RAQWEMPQ V KESKRQFIFD VVNEKMELFV SFCEDTIFEM QIAAQ(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)EVQRVKF LNYLSRNFYT LRFLALFLAF AINFILLF Y KVSDSPPVYY FLEESTGYME PALRCLSLLH TLVAFLCIIG YNCLKVPLVI FKREKELARK LEFDGLYITE QPEDDDVKG QWDRLVLNTP SFPSNYWDKF VKRKVLDKHG DIYGRERIAE IDVKYQIWKF GVIFTDNSFL YLGWYMVMSL LGHYNNFFFA AHLLDIAMG VKTLRTILSS VTHNGKQLVM TVGLLAVVVY LYTVVAFNFF RKFYNKMKCD DMMTCYLFHM YVGVRAGGGI G DEIEDPAG DEYELYRVVF DITFFFFVIV ILLAIIQGLI IDAFGELRDQ QEQVREDMET KCFICGIGSD YFDTTPHRFE TH TLEEHNL ANYMFFLMYL INKDETEHTG QESYVWKMYQ ERCWDFFPAG DCFRKQYEDQ L |
-Macromolecule #3: Calmodulin-1
Macromolecule | Name: Calmodulin-1 / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 16.723365 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREA FRVFDKDGNG YISAAELRHV MTNLGEKLTD EEVDEMIREA DIDGDGQVNY EEFVQMMTA UniProtKB: Calmodulin-1 |
-Macromolecule #4: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 4 / Number of copies: 4 / Formula: ZN |
---|---|
Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 7.5 |
---|---|
Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: DIFFRACTION |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
-
Image processing
Startup model | Type of model: PDB ENTRY |
---|---|
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: PHENIX (ver. dev-3714) / Number images used: 25122 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |