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Open data
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Basic information
Entry | Database: PDB / ID: 9iah | |||||||||||||||||||||||||||
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Title | Structure of beta-lactoglobulin fibril | |||||||||||||||||||||||||||
![]() | Beta-lactoglobulin | |||||||||||||||||||||||||||
![]() | BIOSYNTHETIC PROTEIN / Whey protein / Nutrient transport / Amyloid fibrillation / Cross-beta structure / Nanomaterial | |||||||||||||||||||||||||||
Function / homology | ![]() retinol binding / long-chain fatty acid binding / extracellular region / identical protein binding Similarity search - Function | |||||||||||||||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.17 Å | |||||||||||||||||||||||||||
![]() | Sternke-Hoffmann, R. / Rhyner, D. / Qureshi, B. / Riek, R. / Greenwald, J. / Luo, J. | |||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural Insights and Functional Dynamics of Beta-Lactoglobulin Fibrils Authors: Sternke-Hoffmann, R. / Rhyner, D. / Juranyi, F. / Qureshi, B. / Riek, R. / Greenwald, J. / Luetz-Bueno, V. / Luo, J. | |||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39 KB | Display | ![]() |
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PDB format | ![]() | 27.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 52781MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
#1: Protein/peptide | Mass: 3627.232 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() Has protein modification | N | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
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Sample preparation
Component | Name: Beta-lactoglobulin fibril / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 2.5 |
Buffer component | Conc.: 25 mM / Name: Citric acid-sodium phosphate |
Specimen | Conc.: 7 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: This sample was monodisperse. The sample was prepared at 7 mg/ml and diluted 15 times for EM grid. |
Specimen support | Details: PELCO easiGLOW Glow discharge cleaning system using 25 mA for 30 s. Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % / Chamber temperature: 295.15 K Details: 3.7 ul sample was applied and blotted for 6 s after a wait time of 30 s with a force of 0 |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm / Calibrated defocus min: 500 nm / Calibrated defocus max: 2500 nm / Cs: 2.7 mm / C2 aperture diameter: 100 µm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature (max): 93.15 K / Temperature (min): 88.15 K |
Image recording | Average exposure time: 1 sec. / Electron dose: 57.5 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 2 / Num. of real images: 16475 |
EM imaging optics | Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV |
Image scans | Width: 5760 / Height: 4092 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||
Helical symmerty |
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Particle selection | Num. of particles selected: 1387479 Details: from 3825 micrographs selected based on rlnCtfMaxResolution with a cut-off of 4 A | |||||||||||||||
3D reconstruction | Resolution: 3.17 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 67843 / Symmetry type: HELICAL |