+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-18701 | |||||||||||||||||||||
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Title | Endosomal membrane tethering complex CORVET | |||||||||||||||||||||
Map data | CORVET composite map and associated molecular model | |||||||||||||||||||||
Sample |
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Keywords | CORVET / membrane fusion / endosome / Rab GTPase / tethering / ENDOCYTOSIS | |||||||||||||||||||||
Function / homology | Function and homology information histone catabolic process / organelle fusion / endosomal vesicle fusion / regulation of SNARE complex assembly / CORVET complex / HOPS complex / vesicle tethering / regulation of vacuole fusion, non-autophagic / vacuole inheritance / vacuole fusion, non-autophagic ...histone catabolic process / organelle fusion / endosomal vesicle fusion / regulation of SNARE complex assembly / CORVET complex / HOPS complex / vesicle tethering / regulation of vacuole fusion, non-autophagic / vacuole inheritance / vacuole fusion, non-autophagic / vesicle fusion with vacuole / Golgi to endosome transport / Golgi to vacuole transport / vesicle docking / late endosome to vacuole transport via multivesicular body sorting pathway / endosome organization / vacuole organization / protein targeting to vacuole / late endosome to vacuole transport / Golgi stack / piecemeal microautophagy of the nucleus / fungal-type vacuole / vesicle docking involved in exocytosis / vacuolar acidification / fungal-type vacuole membrane / endosomal transport / lysosome organization / endosome to lysosome transport / protein-membrane adaptor activity / vesicle-mediated transport / intracellular protein transport / RING-type E3 ubiquitin transferase / autophagy / endocytosis / ubiquitin protein ligase activity / late endosome / GTPase binding / protein-macromolecule adaptor activity / actin binding / early endosome membrane / endosome / ATP binding / membrane / metal ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||||||||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | |||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.6 Å | |||||||||||||||||||||
Authors | Shvarev D / Ungermann C / Moeller A / Langemeyer L / Walter S / Perz A / Froehlich F | |||||||||||||||||||||
Funding support | Germany, 6 items
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Citation | Journal: Nat Commun / Year: 2024 Title: Structure of the endosomal CORVET tethering complex. Authors: Dmitry Shvarev / Caroline König / Nicole Susan / Lars Langemeyer / Stefan Walter / Angela Perz / Florian Fröhlich / Christian Ungermann / Arne Moeller / Abstract: Cells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion ...Cells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion steps. Early endosome fusion is promoted by the Rab5 GTPase and its effector, the hexameric CORVET tethering complex, which is homologous to the lysosomal HOPS. How these related complexes recognize their specific target membranes remains entirely elusive. Here, we solve the structure of CORVET by cryo-electron microscopy and revealed its minimal requirements for membrane tethering. As expected, the core of CORVET and HOPS resembles each other. However, the function-defining subunits show marked structural differences. Notably, we discover that unlike HOPS, CORVET depends not only on Rab5 but also on phosphatidylinositol-3-phosphate (PI3P) and membrane lipid packing defects for tethering, implying that an organelle-specific membrane code enables fusion. Our data suggest that both shape and membrane interactions of CORVET and HOPS are conserved in metazoans, thus providing a paradigm how tethering complexes function. | |||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_18701.map.gz | 224.8 MB | EMDB map data format | |
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Header (meta data) | emd-18701-v30.xml emd-18701.xml | 22.9 KB 22.9 KB | Display Display | EMDB header |
Images | emd_18701.png | 60.4 KB | ||
Filedesc metadata | emd-18701.cif.gz | 9.4 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-18701 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-18701 | HTTPS FTP |
-Validation report
Summary document | emd_18701_validation.pdf.gz | 440.8 KB | Display | EMDB validaton report |
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Full document | emd_18701_full_validation.pdf.gz | 440.3 KB | Display | |
Data in XML | emd_18701_validation.xml.gz | 7.2 KB | Display | |
Data in CIF | emd_18701_validation.cif.gz | 8.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18701 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18701 | HTTPS FTP |
-Related structure data
Related structure data | 8qx8MC 7zu0C C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_18701.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | CORVET composite map and associated molecular model | ||||||||||||||||||||
Voxel size | X=Y=Z: 2.037 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : Endosomal membrane tethering complex CORVET
Entire | Name: Endosomal membrane tethering complex CORVET |
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Components |
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-Supramolecule #1: Endosomal membrane tethering complex CORVET
Supramolecule | Name: Endosomal membrane tethering complex CORVET / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
-Macromolecule #1: Vacuolar protein sorting-associated protein 8
Macromolecule | Name: Vacuolar protein sorting-associated protein 8 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Molecular weight | Theoretical: 148.102172 KDa |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Sequence | String: MEQNGLDHDS RSSIDTTIND TQKTFLEFRS YTQLSEKLAS SSSYTAPPLN EDGPKGVASA VSQGSESVVS WTTLTHVYSI LGAYGGPTC LYPTATYFLM GTSKGCVLIF NYNEHLQTIL VPTLSEDPSI HSIRSPVKSI VICSDGTHVA ASYETGNICI W NLNVGYRV ...String: MEQNGLDHDS RSSIDTTIND TQKTFLEFRS YTQLSEKLAS SSSYTAPPLN EDGPKGVASA VSQGSESVVS WTTLTHVYSI LGAYGGPTC LYPTATYFLM GTSKGCVLIF NYNEHLQTIL VPTLSEDPSI HSIRSPVKSI VICSDGTHVA ASYETGNICI W NLNVGYRV KPTSEPTNGM TPTPALPAVL HIDDHVNKEI TGLDFFGARH TALIVSDRTG KVSLYNGYRR GFWQLVYNSK KI LDVNSSK EKLIRSKLSP LISREKISTN LLSVLTTTHF ALILLSPHVS LMFQETVEPS VQNSLVVNSS ISWTQNCSRV AYS VNNKIS VISISSSDFN VQSASHSPEF AESILSIQWI DQLLLGVLTI SHQFLVLHPQ HDFKILLRLD FLIHDLMIPP NKYF VISRR SFYLLTNYSF KIGKFVSWSD ITLRHILKGD YLGALEFIES LLQPYCPLAN LLKLDNNTEE RTKQLMEPFY NLSLA ALRF LIKKDNADYN RVYQLLMVVV RVLQQSSKKL DSIPSLDVFL EQGLEFFELK DNAVYFEVVA NIVAQGSVTS ISPVLF RSI IDYYAKEENL KVIEDLIIML NPTTLDVDLA VKLCQKYNLF DLLIYIWNKI FDDYQTPVVD LIYRISNQSE KCVIFNG PQ VPPETTIFDY VTYILTGRQY PQNLSISPSD KCSKIQRELS AFIFSGFSIK WPSNSNHKLY ICENPEEEPA FPYFHLLL K SNPSRFLAML NEVFEASLFN DDNDMVASVG EAELVSRQYV IDLLLDAMKD TGNSDNIRVL VAIFIATSIS KYPQFIKVS NQALDCVVNT ICSSRVQGIY EISQIALESL LPYYHSRTTE NFILELKEKN FNKVLFHIYK SENKYASALS LILETKDIEK EYNTDIVSI TDYILKKCPP GSLECGKVTE VIETNFDLLL SRIGIEKCVT IFSDFDYNLH QEILEVKNEE TQQKYLDKLF S TPNINNKV DKRLRNLHIE LNCKYKSKRE MILWLNGTVL SNAESLQILD LLNQDSNFEA AAIIHERLES FNLAVRDLLS FI EQCLNEG KTNISTLLES LRRAFDDCNS AGTEKKSCWI LLITFLITLY GKYPSHDERK DLCNKLLQEA FLGLVRSKSS SQK DSGGEF WEIMSSVLEH QDVILMKVQD LKQLLLNVFN TYKLERSLSE LIQKIIEDSS QDLVQQYRKF LSEGWSIHTD DCEI CGKKI WGAGLDPLLF LAWENVQRHQ DMISVDLKTP LVIFKCHHGF HQTCLENLAQ KPDEYSCLIC QTESNPKIVD YKDDD DKDY KDDDDKDYKD DDDK UniProtKB: Vacuolar protein sorting-associated protein 8 |
-Macromolecule #2: Vacuolar protein sorting-associated protein 33
Macromolecule | Name: Vacuolar protein sorting-associated protein 33 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Molecular weight | Theoretical: 79.354977 KDa |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Sequence | String: MNRFWNTKKF SLTNADGLCA TLNEISQNDE VLVVQPSVLP VLNSLLTFQD LTQSTPVRKI TLLDDQLSDD LPSALGSVPQ MDLIFLIDV RTSLRLPPQL LDAAQKHNLS SLHIIYCRWK PSFQNTLEDT EQWQKDGFDL NSKKTHFPNV IESQLKELSN E YTLYPWDL ...String: MNRFWNTKKF SLTNADGLCA TLNEISQNDE VLVVQPSVLP VLNSLLTFQD LTQSTPVRKI TLLDDQLSDD LPSALGSVPQ MDLIFLIDV RTSLRLPPQL LDAAQKHNLS SLHIIYCRWK PSFQNTLEDT EQWQKDGFDL NSKKTHFPNV IESQLKELSN E YTLYPWDL LPFPQIDENV LLTHSLYNME NVNMYYPNLR SLQSATESIL VDDMVNSLQS LIFETNSIIT NVVSIGNLSK RC SHLLKKR IDEHQTENDL FIKGTLYGER TNCGLEMDLI ILERNTDPIT PLLTQLTYAG ILDDLYEFNS GIKIKEKDMN FNY KEDKIW NDLKFLNFGS IGPQLNKLAK ELQTQYDTRH KAESVHEIKE FVDSLGSLQQ RQAFLKNHTT LSSDVLKVVE TEEY GSFNK ILELELEILM GNTLNNDIED IILELQYQYE VDQKKILRLI CLLSLCKNSL REKDYEYLRT FMIDSWGIEK CFQLE SLAE LGFFTSKTGK TDLHITTSKS TRLQKEYRYI SQWFNTVPIE DEHAADKITN ENDDFSEATF AYSGVVPLTM RLVQML YDR SILFHNYSSQ QPFILSREPR VSQTEDLIEQ LYGDSHAIEE SIWVPGTITK KINASIKSNN RRSIDGSNGT FHAAEDI AL VVFLGGVTMG EIAIMKHLQK ILGKKGINKR FIIIADGLIN GTRIMNSIS UniProtKB: Vacuolar protein sorting-associated protein 33 |
-Macromolecule #3: Vacuolar protein sorting-associated protein 16
Macromolecule | Name: Vacuolar protein sorting-associated protein 16 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Molecular weight | Theoretical: 92.857 KDa |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Sequence | String: MKNPSFDWER LKDVFYRSRA IGELKWPTQY EEFKCALSLT VIAVEIQDFI QVYNYFGQLL GKINLQRIHE DIIKFEFDKD EKLILVTKS SIKIVKGWSP LTIESVPLQD PTIDTIWDYH NGIMLLAKSR DIYKLNGNEW ELLYENKDKK YNLLTKNHWS C NDDSIILL ...String: MKNPSFDWER LKDVFYRSRA IGELKWPTQY EEFKCALSLT VIAVEIQDFI QVYNYFGQLL GKINLQRIHE DIIKFEFDKD EKLILVTKS SIKIVKGWSP LTIESVPLQD PTIDTIWDYH NGIMLLAKSR DIYKLNGNEW ELLYENKDKK YNLLTKNHWS C NDDSIILL DVDHVYQVST SNGALLKLIT DSSWHKVTIS SRGFICLYNM KDNKLQIFRD PARILMEHNL DSTPDDICWC GN DTVACSF EDEIKLYGPD GLYVTFWYPF TVTNLRAEVD GLKVITTEKI YFLSRVQPQT SNIFRIGSTE PGAMLVDSFS LLE DHAPKA IEILKNFVLE KGVLDCIAAA IDEFEPKLQK MLLNAASYGK ASLQYKSFDA SIFVNACNTI KLLNCFRSFG IFLT VEEYR CISLKGVIDR LLKYHRYYEC IQICKLANER FLLGYVFTEW AKDKIKGSPD MEDDELLDKI KSRLSVIDMT DTLQM VAVA KVAYLEGRFQ LSRNLALLEK NEEARIEQLY NLDDDSIALK ECIKVQNYSL TISLLIALSK KLTNSQLTKL LIIDMF NNP LYLYYMRMDK AYLYDFYRQT DRFIDLAHVL LQQGKEQQSL HSFLPQIKDL YSQVQNSEVV NNTIEQLQRQ EKLWIYQ ES LGKRFAISFT NMTLDQTLSK LIETGQDKQV KEIVKKFKIS EKKLYHLKCK TLVEAKKFDE LLQFAQSRKS PIGYMPFY T YLKSRGHMDK ASPYVNMIPG LSYQEKKKLY VECRGFRDAI QLAGKEKDIP GLKEIYNIIP PNEPELKALA NETMSRI UniProtKB: Vacuolar protein sorting-associated protein 16 |
-Macromolecule #4: E3 ubiquitin-protein ligase PEP5
Macromolecule | Name: E3 ubiquitin-protein ligase PEP5 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Molecular weight | Theoretical: 117.617219 KDa |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Sequence | String: MSLSSWRQFQ LFENIPIRDP NFGGDSLLYS DPTLCAATIV DPQTLIIAVN SNIIKVVKLN QSQVIHEFQS FPHDFQITFL KVINGEFLV ALAESIGKPS LIRVYKLEKL PNREQLYHSQ VELKNGNNTY PISVVSISND LSCIVVGFIN GKIILIRGDI S RDRGSQQR ...String: MSLSSWRQFQ LFENIPIRDP NFGGDSLLYS DPTLCAATIV DPQTLIIAVN SNIIKVVKLN QSQVIHEFQS FPHDFQITFL KVINGEFLV ALAESIGKPS LIRVYKLEKL PNREQLYHSQ VELKNGNNTY PISVVSISND LSCIVVGFIN GKIILIRGDI S RDRGSQQR IIYEDPSKEP ITALFLNNDA TACFAATTSR ILLFNTTGRN RGRPSLVLNS KNGLDLNCGS FNPATNEFIC CL SNFIEFF SSSGKKHQFA FDLSLRKRIF CVDKDHILIV TEETGVPTTS ISVNELSPTI INRIFIIDAK NKIISLNFVV SSA IIDIFS TSQSGKNITY LLTSEGVMHR ITPKSLENQI NIIIQKELYP FALQLAKQHS LSPLDVQEIH KKYGDYLFKK GLRK EATDQ YIQCLDVVET SEIISKFGVK EVPDPESMRN LADYLWSLIK NSISQRDHVT LLLIVLIKLK DVEGIDTFIQ HFDRK GIWN EGVVMDDMDD VTFFYSDNDF FDLDLILELM KESDFKRLSY RLAKKYSKDS LIIVDILLNL LHNPVKAIKY IKSLPI DET LRCLVTYSKK LLEESPNETN ALLIEVFTGK FKPSTFEVDL DRRDTTGDFS ENIRTVFYSY KTFFNYMNSN GTSDAMS ES SEASHEHEEP TYHPPKPSIV FSSFVTKPFE FVVFLEACLA CYQQYEGFDE DRQVILTTLY DLYLNLAQND VPERIDDW R SRATGVLRES NKLVYSAASN NTSKRVDNSI MLLISHMDQS SASAKDKTKI DIASFANDNP EMDLLSTFRA MTLNEEPST CLKFLEKYGT EEPKLLQVAL SYFVSNKLIF KEMGGNEVLK EKVLRPIIEG ERMPLLDIIK ALSRTNVAHF GLIQDIIIDH VKTEDTEIK RNEKLIESYD KELKEKNKKL KNTINSDQPL HVPLKNQTCF MCRLTLDIPV VFFKCGHIYH QHCLNEEEDT L ESERKLFK CPKCLVDLET SNKLFEAQHE VVEKNDLLNF ALNSEEGSRD RFKVITEFLG RGAISYSDIT I UniProtKB: E3 ubiquitin-protein ligase PEP5 |
-Macromolecule #5: Vacuolar protein sorting-associated protein 3
Macromolecule | Name: Vacuolar protein sorting-associated protein 3 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Molecular weight | Theoretical: 117.069008 KDa |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Sequence | String: MVKKKTNNDK GKEVKENEGK LDIDSESSPH ERENDKKKTE DDSLRATESE ETNTHNANPN ETVRADKFSQ EESRPIEDSP HTDKNTAQE SCQPSSAEDN VINTDITSLN EKTSTNDEQE KGLPLKISEG PFTISTLLDN VPSDLIYTCC EAYENHIFLG T TTGDLLHY ...String: MVKKKTNNDK GKEVKENEGK LDIDSESSPH ERENDKKKTE DDSLRATESE ETNTHNANPN ETVRADKFSQ EESRPIEDSP HTDKNTAQE SCQPSSAEDN VINTDITSLN EKTSTNDEQE KGLPLKISEG PFTISTLLDN VPSDLIYTCC EAYENHIFLG T TTGDLLHY FELERGNYML VSQTKFDAES NSKIDKILLL PKVEGALILC DNELVLFILP EFAPRPNTTR LKGISDVVIC NF SRSSKAY RIYAFHAEGV RLLKISADSL VLTKAFNFKL IDKACAHEET LMVSKLNSYE LINLKSSQVI PLFRISETDE DLE PIITSF NEQSEFLVCS GGGSYDSGAM ALVVNHHGDI IKGTIVLKNY PRNVIVEFPY IIAESAFQSV DIYSALPSEK SQLL QSITT SGSDLKISKS DNVFTNTNNS EEFKEKIFNK LRLEPLTHSD NKFRIERERA FVEESYEEKT SLIVYNNLGI HLLVP TPMV LRFTSCEESE IDNIEDQLKK LAKKDLTKFE HIEAKYLMSL LLFLMTLHYD HIEDEVMKKW CDFSDKVDIR ILFYMF GWK VYSEIWCFHG LINIVERLKS LKLTNKCENI LKMLLMMKNE LKKKNKTGLL TNDFDDIMKT IDITLFKLRL EKKETIT VD MFERESYDEI IREINLHDDK LPRIELLIEI YKEKGEYLKA LNLLREAGDY ISLVSFIEEN LKKLPEDYIK ERIADDLL L TLKQGDENTE ECAIKKVLKI LDMACINKND FLNKIPAEET SLKVSFIEQL GVQNSNDSKF LFNYYLAKLR EIINQSNIW SILGDFIKEY KDDFAYDKTD ITNFIHIKLK HSLQCENFSK YYEKCENLKS ENEKDDEFIN FTFDEISKID KEHILTLLFF PNELTNWVS SEELLKIYLS FNDFRSVEKY IGKQNLVAVM KQYLDISSLN YSVELVTNLL QRNFELLDDT DIQLKILETI P SVFPVQTI SELLLKVLIK YQEKKEESNL RKCLLKNQIS ISDELSRNFD SQG UniProtKB: Vacuolar protein sorting-associated protein 3 |
-Macromolecule #6: Vacuolar membrane protein PEP3
Macromolecule | Name: Vacuolar membrane protein PEP3 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Molecular weight | Theoretical: 107.531047 KDa |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Sequence | String: MIKTRIEEVQ LQFLTGNTEL THLKVSNDQL IVTTQRTIYR INLQDPAIVN HFDCPLSKEL ETIMNVHVSP MGSVILIRTN FGRYMLLKD GEFTQLNKIK NLDLSSLHWI NETTFLMGIK KTPKLYRVEL TGKDITTKLW YENKKLSGGI DGIAYWEGSL L LTIKDNIL ...String: MIKTRIEEVQ LQFLTGNTEL THLKVSNDQL IVTTQRTIYR INLQDPAIVN HFDCPLSKEL ETIMNVHVSP MGSVILIRTN FGRYMLLKD GEFTQLNKIK NLDLSSLHWI NETTFLMGIK KTPKLYRVEL TGKDITTKLW YENKKLSGGI DGIAYWEGSL L LTIKDNIL YWRDVTNMKF PLVLPDESEQ FERLKHHAIK KFDSYNGLFA WVTSNGIVFG DLKEKQMEKD PASNNFGKFL SS SKVLLNF ELPDYQNDKD HLIKDIVLTA FHILLLRKNT VTMVSQLNND VVFHETIPRH QLTGSNTDSN EKFLGLVRDS VKE TFWCFS NINVFEIIIE NEPNSVWNLL VRDNKFDKAL SLKGLTVREI ESVKLSKAMY LFHTAKDFHS AAQTLGSMKD LSHF GEIAL NFLQIKDYND LNVILIKQLD NVPWKSTQVV LSSWIIWNFM KQLNDIELKI NTTKPASTDE DNLLNWNLNL KEKSN ELTK FLESHLEKLD NETVYQIMSK QNRQNELLIF ASLINDMKFL LSFWIDQGNW YESLKILLTI NNHDLVYKYS LILLLN SPE ATVSTWMKIK DLDPNKLIPT ILKFFTNWQN NSKLITNISE YPENYSLTYL KWCVREVPKM CNPIVYNSIL YMMITDP RN DMILENDIIK FMKSNENKYD LNFQLRLSLK FKKTKTSIFL LTRLNLFEDA IDLALKNNLI DDCKVIVNDE ILIEDYKL R KRLWLKIAKH LLLSMKDIDI KQLIRTILND SNEILTIKDL LPFFNEYTTI ANLKEELIKF LENHNMKMNE ISEDIINSK NLKVEINTEI SKFNEIYRIL EPGKSCDECG KFLQIKKFIV FPCGHCFHWN CIIRVILNSN DYNLRQKTEN FLKAKSKHNL NDLENIIVE KCGLCSDINI NKIDQPISID ETELAKWNE UniProtKB: Vacuolar membrane protein PEP3 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm |
Sample stage | Cooling holder cryogen: NITROGEN |
-Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 219391 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |