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Open data
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Basic information
Entry | Database: PDB / ID: 5k7p | ||||||
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Title | MicroED structure of xylanase at 2.3 A resolution | ||||||
![]() | Endo-1,4-beta-xylanase 2![]() | ||||||
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Function / homology | ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | de la Cruz, M.J. / Hattne, J. / Shi, D. / Seidler, P. / Rodriguez, J. / Reyes, F.E. / Sawaya, M.R. / Cascio, D. / Eisenberg, D. / Gonen, T. | ||||||
![]() | ![]() Title: Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED. Authors: M Jason de la Cruz / Johan Hattne / Dan Shi / Paul Seidler / Jose Rodriguez / Francis E Reyes / Michael R Sawaya / Duilio Cascio / Simon C Weiss / Sun Kyung Kim / Cynthia S Hinck / Andrew P ...Authors: M Jason de la Cruz / Johan Hattne / Dan Shi / Paul Seidler / Jose Rodriguez / Francis E Reyes / Michael R Sawaya / Duilio Cascio / Simon C Weiss / Sun Kyung Kim / Cynthia S Hinck / Andrew P Hinck / Guillermo Calero / David Eisenberg / Tamir Gonen / ![]() Abstract: Traditionally, crystallographic analysis of macromolecules has depended on large, well-ordered crystals, which often require significant effort to obtain. Even sizable crystals sometimes suffer from ...Traditionally, crystallographic analysis of macromolecules has depended on large, well-ordered crystals, which often require significant effort to obtain. Even sizable crystals sometimes suffer from pathologies that render them inappropriate for high-resolution structure determination. Here we show that fragmentation of large, imperfect crystals into microcrystals or nanocrystals can provide a simple path for high-resolution structure determination by the cryoEM method MicroED and potentially by serial femtosecond crystallography. | ||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 51.2 KB | Display | ![]() |
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PDB format | ![]() | 34.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 8218MC ![]() 8216C ![]() 8217C ![]() 8219C ![]() 8220C ![]() 8221C ![]() 8222C ![]() 8472C ![]() 5k7nC ![]() 5k7oC ![]() 5k7qC ![]() 5k7rC ![]() 5k7sC ![]() 5k7tC ![]() 5ty4C M: map data used to model this data C: citing same article ( |
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Similar structure data | |
Experimental dataset #1 | Data reference: ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | ![]() Mass: 20855.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() ![]() | ||
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#2: Chemical | ![]() #3: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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EM experiment | Aggregation state: 3D ARRAY / 3D reconstruction method: ![]() |
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Sample preparation
Component | Name: Xylanase![]() | ||||||||||||||||||||
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Molecular weight | Value: 0.021035 MDa / Experimental value: NO | ||||||||||||||||||||
Source (natural) | Organism: ![]() ![]() | ||||||||||||||||||||
Buffer solution | pH: 9 | ||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied![]() ![]() | ||||||||||||||||||||
Vitrification![]() | Cryogen name: ETHANE |
-Data collection
Experimental equipment | ![]() Model: Tecnai F20 / Image courtesy: FEI Company | ||||||||||||||||||||||||
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Microscopy | Model: FEI TECNAI F20 | ||||||||||||||||||||||||
Electron gun | Electron source![]() ![]() | ||||||||||||||||||||||||
Electron lens | Mode: DIFFRACTION![]() | ||||||||||||||||||||||||
Specimen holder | Cryogen: NITROGEN | ||||||||||||||||||||||||
Image recording | Average exposure time: 4.1 sec. / Electron dose: 0.004 e/Å2 / Film or detector model: TVIPS TEMCAM-F416 (4k x 4k) / Num. of diffraction images: 588 / Num. of grids imaged: 1 / Num. of real images: 588 | ||||||||||||||||||||||||
Image scans | Sampling size: 0.0311999992 µm / Width: 2048 / Height: 2048 | ||||||||||||||||||||||||
EM diffraction | Camera length: 1750 mm | ||||||||||||||||||||||||
EM diffraction shell | Resolution: 2.3→2.63 Å / Fourier space coverage: 74.9 % / Multiplicity: 3.8 / Num. of structure factors: 2285 / Phase residual: 53.8 ° | ||||||||||||||||||||||||
EM diffraction stats | Fourier space coverage: 66.6 % / High resolution: 1.9 Å / Num. of intensities measured: 38699 / Num. of structure factors: 10664 / Phase error: 29.95 ° / Phase residual: 44.49 ° / Phase error rejection criteria: 0 / Rmerge: 0.428 / Rsym: 0.428 | ||||||||||||||||||||||||
Reflection | Resolution: 1.9→25.55 Å / Num. all: 38699 / Num. obs: 10664 / % possible obs: 66.6 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.428 / Rpim(I) all: 0.245 / Net I/σ(I): 2.7 | ||||||||||||||||||||||||
Reflection shell |
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Processing
Software | Name: PHENIX / Version: (1.10_2155: ???) / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
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EM software |
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EM 3D crystal entity | ∠α: 90 ° / ∠β: 90 ° / ∠γ: 90 ° / A: 49.1 Å / B: 59.02 Å / C: 70 Å / Space group name: P212121 / Space group num: 19 | ||||||||||||||||||||||||||||||||||||||||
CTF correction![]() | Type: NONE | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction![]() | Resolution: 2.3 Å / Resolution method: DIFFRACTION PATTERN/LAYERLINES / Symmetry type: 3D CRYSTAL | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: OTHER / Space: RECIPROCAL | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 2DFB Pdb chain-ID: A / Accession code: 2DFB / Pdb chain residue range: 1-190 / Source name: PDB / Type: experimental model | ||||||||||||||||||||||||||||||||||||||||
Refinement | Resolution: 2.3→25.549 Å / SU ML: 0.42 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.95 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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LS refinement shell |
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