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Open data
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Basic information
Entry | ![]() | |||||||||||||||
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Title | C1 reconstruction of augmin T-II bonsai on the microtubule | |||||||||||||||
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![]() | Microtubule / augmin / CH / spindle / CELL CYCLE | |||||||||||||||
Function / homology | ![]() HAUS complex / microtubule minus-end binding / microtubule organizing center organization / mitotic spindle microtubule / positive regulation of axon guidance / centrosome cycle / microtubule-based process / spindle assembly / cytoplasmic microtubule / cellular response to interleukin-4 ...HAUS complex / microtubule minus-end binding / microtubule organizing center organization / mitotic spindle microtubule / positive regulation of axon guidance / centrosome cycle / microtubule-based process / spindle assembly / cytoplasmic microtubule / cellular response to interleukin-4 / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / spindle pole / mitotic cell cycle / double-stranded RNA binding / microtubule cytoskeleton / microtubule binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / cilium / protein heterodimerization activity / cell division / GTPase activity / ubiquitin protein ligase binding / centrosome / GTP binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | ![]() ![]() ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.83 Å | |||||||||||||||
![]() | Travis SM / Zhang R | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: How augmin establishes the angle of the microtubule branch site Authors: Travis SM / Kraus J / McManus CT / Golden J / Zhang R / Petry S | |||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 123 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 28.1 KB 28.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.2 KB | Display | ![]() |
Images | ![]() | 143.3 KB | ||
Masks | ![]() | 244.1 MB | ![]() | |
Filedesc metadata | ![]() | 7.5 KB | ||
Others | ![]() ![]() | 226.8 MB 226.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 22.4 KB | Display | |
Data in CIF | ![]() | 29.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9d2bC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.426 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_46488_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_46488_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Augmin T-II bonsai on the microtubule
Entire | Name: Augmin T-II bonsai on the microtubule |
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Components |
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-Supramolecule #1: Augmin T-II bonsai on the microtubule
Supramolecule | Name: Augmin T-II bonsai on the microtubule / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Complex of augmin bound to the microtubule |
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Molecular weight | Theoretical: 92 KDa |
-Supramolecule #2: GMPCPP microtubule
Supramolecule | Name: GMPCPP microtubule / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#2 Details: bovine tubulin polymerized in the presence of GMPCPP |
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Source (natural) | Organism: ![]() ![]() |
-Supramolecule #3: augmin T-II bonsai
Supramolecule | Name: augmin T-II bonsai / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #3-#5 / Details: trimeric fragment of Xenopus laevis augmin |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: TUBA1
Macromolecule | Name: TUBA1 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS ...String: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y UniProtKB: Tubulin alpha-1B chain |
-Macromolecule #2: TUBB2
Macromolecule | Name: TUBB2 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM ...String: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA UniProtKB: Tubulin beta-2B chain |
-Macromolecule #3: HAUS6.L
Macromolecule | Name: HAUS6.L / type: protein_or_peptide / ID: 3 / Details: N-terminal 6xHis / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGSSHHHHHH SGRENLYFQG SMQSGSRPHL AWQREHMWLA LQGLGFESGA EAANAGKTLV HVTFGVNMFD KPNKDAFYVV FHFLFGKLDN VRCKEVFRYC WPPLDKKRDA EFRKACCEWL KKISDEVGAG FPQVVASIFL SPGGPKFVHL LYHFARYVML QHIKRDADAG ...String: MGSSHHHHHH SGRENLYFQG SMQSGSRPHL AWQREHMWLA LQGLGFESGA EAANAGKTLV HVTFGVNMFD KPNKDAFYVV FHFLFGKLDN VRCKEVFRYC WPPLDKKRDA EFRKACCEWL KKISDEVGAG FPQVVASIFL SPGGPKFVHL LYHFARYVML QHIKRDADAG NVFISEALQS KIQDPQKALA RNKLARQKYL KVLQKENLVI EEYQRKAQLL IKQIRDMRSE HVALQNQQKL AEKVDRKISD KDENIQKTRC MWNTIMQMLK EMEKEVDVVD AVVRGNIDQ UniProtKB: HAUS augmin like complex subunit 6 L homeolog isoform X1 |
-Macromolecule #4: HAUS7.S
Macromolecule | Name: HAUS7.S / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MADPWSHPQF EKGGTGGKEL GAAVELYERL QMLSCPCLEG VYLTDPQSIY ELLCTPSSHR LDILQWLCSR IYPPVQEQLS SLKESQTDTK VKEIAKLCFD LMLCHFDDLD LIRGHASPFK QISFIGQLLD VIQYPDTISS NVILESLSHS TEKNVVTCIR ENEELLKELF ...String: MADPWSHPQF EKGGTGGKEL GAAVELYERL QMLSCPCLEG VYLTDPQSIY ELLCTPSSHR LDILQWLCSR IYPPVQEQLS SLKESQTDTK VKEIAKLCFD LMLCHFDDLD LIRGHASPFK QISFIGQLLD VIQYPDTISS NVILESLSHS TEKNVVTCIR ENEELLKELF SSPHFQATLS PECNPWPADF KPLLNAEESL QKRATQSSKG KDMSNSVEAL LEISSSLKAL KEECVDLCSS VTDGDKVIQS LRLALTDFHQ LTIAFNQIYA NEFQWSHPQF EK UniProtKB: HAUS augmin like complex subunit 7 S homeolog |
-Macromolecule #5: HAUS8.L
Macromolecule | Name: HAUS8.L / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MRSMSEAGVA PIEDGSQNSS GGSSGDAALK KSKGGAKVVK SRYMQIGRSK VSKNSLANTT VCSGGKVPER GSGGTPTRRS LAPHKAKITA AVPLPALDGS IFTKEDLQST LLDGHRIARP DLDLSVINDR TLQKITPRPV VTSEQKKPKR DTTPVNLVPE DMVEMIESQT ...String: MRSMSEAGVA PIEDGSQNSS GGSSGDAALK KSKGGAKVVK SRYMQIGRSK VSKNSLANTT VCSGGKVPER GSGGTPTRRS LAPHKAKITA AVPLPALDGS IFTKEDLQST LLDGHRIARP DLDLSVINDR TLQKITPRPV VTSEQKKPKR DTTPVNLVPE DMVEMIESQT LLLTYLTIKM QKNLFRLEEK AERNLLLVND QKDQLQETIH MMKRDLTLLQ REERLRDLIE KQDEVLTPVV TSKDPFKDNY TTFATALDST UniProtKB: HAUS augmin-like complex subunit 8 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 6.8 Component:
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Grid | Model: Quantifoil / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 10 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.037 kPa | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 85 % / Chamber temperature: 298 K / Instrument: LEICA EM GP | |||||||||||||||
Details | 20 uM tubulin, 10 uM augmin T-II bonsai |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: TFS Selectris / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number grids imaged: 1 / Number real images: 2088 / Average exposure time: 4.1 sec. / Average electron dose: 15.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 0.1 mm / Nominal defocus max: 3.5 µm / Nominal defocus min: 2.0 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model |
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Refinement | Space: REAL / Protocol: FLEXIBLE FIT / Overall B value: 36.83 |