+Open data
-Basic information
Entry | Database: PDB / ID: 4uzz | ||||||
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Title | Crystal structure of the TtIFT52-46 complex | ||||||
Components |
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Keywords | MOTOR PROTEIN / CILIUM / IFT / INTRACELLULAR TRANSPORT / FLAGELLUM | ||||||
Function / homology | Function and homology information | ||||||
Biological species | TETRAHYMENA THERMOPHILA (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.318 Å | ||||||
Authors | Braeuer, P. / Taschner, M. / Lorentzen, E. | ||||||
Citation | Journal: J.Cell Biol. / Year: 2014 Title: Crystal Structures of Ift70/52 and Ift52/46 Provide Insight Into Intraflagellar Transport B Core Complex Assembly. Authors: Taschner, M. / Kotsis, F. / Braeuer, P. / Kuehn, E.W. / Lorentzen, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4uzz.cif.gz | 46.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4uzz.ent.gz | 33.2 KB | Display | PDB format |
PDBx/mmJSON format | 4uzz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4uzz_validation.pdf.gz | 433.1 KB | Display | wwPDB validaton report |
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Full document | 4uzz_full_validation.pdf.gz | 436.7 KB | Display | |
Data in XML | 4uzz_validation.xml.gz | 8.5 KB | Display | |
Data in CIF | 4uzz_validation.cif.gz | 10.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uz/4uzz ftp://data.pdbj.org/pub/pdb/validation_reports/uz/4uzz | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 13460.124 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN, RESIDUES 221-332 Source method: isolated from a genetically manipulated source Source: (gene. exp.) TETRAHYMENA THERMOPHILA (eukaryote) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q23KH7 |
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#2: Protein | Mass: 7712.705 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN, RESIDUES 371-434 Source method: isolated from a genetically manipulated source Source: (gene. exp.) TETRAHYMENA THERMOPHILA (eukaryote) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: I7LT74 |
#3: Water | ChemComp-HOH / |
Sequence details | GAAS IS A LEFTOVER SEQUENCE FROM THE N-TERMINAL AFFINITY TAG |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.6 Å3/Da / Density % sol: 73 % / Description: NONE |
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Crystal grow | pH: 8.2 / Details: 50MM TRISD PH 8.2, 0.6M TRI-SODIUM- CITRATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 21, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.32→40 Å / Num. obs: 17160 / % possible obs: 99 % / Observed criterion σ(I): -3 / Redundancy: 6.2 % / Biso Wilson estimate: 71.12 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 17 |
Reflection shell | Resolution: 2.32→2.4 Å / Redundancy: 5.4 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 0.6 / % possible all: 92.9 |
-Processing
Software |
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Refinement | Method to determine structure: SAD Starting model: NONE Resolution: 2.318→42.197 Å / SU ML: 0.32 / σ(F): 1.33 / Phase error: 38.81 / 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 | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.318→42.197 Å
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Refine LS restraints |
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LS refinement shell |
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