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Yorodumi- EMDB-3994: Morphology X - cross-beta amyloid fibril structure from the IGSNV... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-3994 | |||||||||
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| Title | Morphology X - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM | |||||||||
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Sample |
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| Biological species | Homo sapiens (human) | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 17.7 Å | |||||||||
Authors | Close W / Faendrich M | |||||||||
Citation | Journal: Nat Commun / Year: 2018Title: Physical basis of amyloid fibril polymorphism. Authors: William Close / Matthias Neumann / Andreas Schmidt / Manuel Hora / Karthikeyan Annamalai / Matthias Schmidt / Bernd Reif / Volker Schmidt / Nikolaus Grigorieff / Marcus Fändrich / ![]() Abstract: Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based ...Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based reconstructions from different fibril morphologies formed by a peptide fragment from an amyloidogenic immunoglobulin light chain. The observed fibril morphologies vary in the number and cross-sectional arrangement of a structurally conserved building block. A comparison with the theoretically possible constellations reveals the experimentally observed spectrum of fibril morphologies to be governed by opposing sets of forces that primarily arise from the β-sheet twist, as well as peptide-peptide interactions within the fibril cross-section. Our results provide a framework for rationalizing and predicting the structure and polymorphism of cross-β fibrils, and suggest that a small number of physical parameters control the observed fibril architectures. | |||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_3994.map.gz | 66.8 MB | EMDB map data format | |
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| Header (meta data) | emd-3994-v30.xml emd-3994.xml | 10.2 KB 10.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_3994_fsc.xml | 23.7 KB | Display | FSC data file |
| Images | emd_3994.png | 51.1 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-3994 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-3994 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 3986C ![]() 3987C ![]() 3988C ![]() 3989C ![]() 3990C ![]() 3991C ![]() 3992C ![]() 3993C C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_3994.map.gz / Format: CCP4 / Size: 84.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.05 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Amyloidogenic Fragment IGSNVVTWYQQL of Immunoglobulin Light Chain...
| Entire | Name: Amyloidogenic Fragment IGSNVVTWYQQL of Immunoglobulin Light Chain of a Human AL Patient |
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| Components |
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-Supramolecule #1: Amyloidogenic Fragment IGSNVVTWYQQL of Immunoglobulin Light Chain...
| Supramolecule | Name: Amyloidogenic Fragment IGSNVVTWYQQL of Immunoglobulin Light Chain of a Human AL Patient type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: Homo sapiens (human) |
| Recombinant expression | Organism: synthetic construct (others) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | helical reconstruction |
| Aggregation state | filament |
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Sample preparation
| Concentration | 5.00 mg/mL |
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| Buffer | pH: 8 / Component - Concentration: 50.0 mM / Component - Name: Tris |
| Grid | Model: C-flat-1.2/1.3 / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 50 % / Instrument: GATAN CRYOPLUNGE 3 Details: Incubation of fibril solution on glow discharged holey carbon grid for 30 seconds and backside blotting for 4 seconds before plunging. |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Dimensions - Width: 7420 pixel / Digitization - Dimensions - Height: 7676 pixel / Digitization - Frames/image: 1-73 / Number real images: 458 / Average exposure time: 21.9 sec. / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi


Homo sapiens (human)
Authors
Citation

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