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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | TTYH2 in complex with sybody 1 in cell-derived vesicles | |||||||||
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![]() | membrane protein / synthetic nanobody / native vesicles | |||||||||
Biological species | synthetic construct (others) / ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 8.23 Å | |||||||||
![]() | Sukalskaia A / Dutzler R / Pugnetti A / Karner A / Weber F / Plochberger B | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Interactions between TTYH2 and ApoE facilitate endosomal lipid transfer Authors: Sukalskaia A / Dutzler R / Pugnetti A / Karner A / Weber F / Plochberger B | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 2.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.5 KB 16.5 KB | Display Display | ![]() |
Images | ![]() | 30.6 KB | ||
Filedesc metadata | ![]() | 5.4 KB | ||
Others | ![]() ![]() | 4.4 MB 4.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 2.604 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_53291_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_53291_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : TTYH2 in complex with a synthetic nanobody residing in cell-deriv...
Entire | Name: TTYH2 in complex with a synthetic nanobody residing in cell-derived vesicles |
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Components |
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-Supramolecule #1: TTYH2 in complex with a synthetic nanobody residing in cell-deriv...
Supramolecule | Name: TTYH2 in complex with a synthetic nanobody residing in cell-derived vesicles type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Molecular weight | Theoretical: 149 KDa |
-Supramolecule #2: Sybody 1
Supramolecule | Name: Sybody 1 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2 |
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Source (natural) | Organism: synthetic construct (others) |
-Supramolecule #3: TTYH2 homodimer
Supramolecule | Name: TTYH2 homodimer / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: TTYH2 homodimer
Macromolecule | Name: TTYH2 homodimer / type: protein_or_peptide / ID: 1 / Details: contains a C-terminal Myc-tag followed by SBP-tag / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: MSQAARVDYI APWWVVWLHS VPHVGLRLQP VNSTFSPGDE SYQESLLFLG LVAAVCLGLN LIFLVAYLVC ACHCRRDDAV QTKQHHSCCI TWTAVVAGLI CCAAVGVGFY GNSETNDGAY QLMYSLDDAN HTFSGIDALV SGTTQKMKVD LEQHLARLSE IFAARGDYLQ ...String: MSQAARVDYI APWWVVWLHS VPHVGLRLQP VNSTFSPGDE SYQESLLFLG LVAAVCLGLN LIFLVAYLVC ACHCRRDDAV QTKQHHSCCI TWTAVVAGLI CCAAVGVGFY GNSETNDGAY QLMYSLDDAN HTFSGIDALV SGTTQKMKVD LEQHLARLSE IFAARGDYLQ TLKFIQQMAG SVVVQLSGLP VWREVTMELT KLSDQTGYVE YYRWLSYLLL FILDLVICLI ACLGLAKRSK CLLASMLCCG ALSLLLSWAS LAADGSAAVA TSDFCVAPDT FILNVTEGQI STEVTRYYLY CSQSGSSPFQ QTLTTFQRAL TTMQIQVAGL LQFAVPLFST AEEDLLAIQL LLNSSESSLH QLTAMVDCRG LHKDYLDALA GICYDGLQGL LYLGLFSFLA ALAFSTMICA GPRAWKHFTT RNRDYDDIDD DDPFNPQAWR MAAHSPPRGQ LHSFCSYSSG LGSQTSLQPP AQTISNAPVS EYMNQAMLFG RNPRYENVPL IGRASPPPTY SPSMRATYLS VADEHLRHYG NQFPAALEVL FQGPQGTEQK LISEEDLRGA SMDEKTTGWR GGHVVEGLAG ELEQLRARLE HHPQGQREP |
-Macromolecule #2: Sybody 1
Macromolecule | Name: Sybody 1 / type: protein_or_peptide / ID: 2 / Details: contains a C-terminal Myc-tag followed by His-tag / Enantiomer: LEVO |
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Source (natural) | Organism: synthetic construct (others) |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAGSSSQVQL VESGGGLVQA GGSLRLSCAA SGFPVTNDSM HWYRQAPGKE REWVAAIASQ GRGTAYADSV KGRFTISRDN AKSTVYLQMN SLKPEDTAVY YCNVKDYGYD LQWYDYWGQG TQVTVSAGRA GEQKLISEED LNSAVDHHHH HH |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 Component:
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Vitrification | Cryogen name: NITROGEN |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 69.33 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |