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Yorodumi- PDB-4w8j: Structure of the full-length insecticidal protein Cry1Ac reveals ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4w8j | ||||||
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Title | Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals | ||||||
Components | Pesticidal crystal protein cry1Ac | ||||||
Keywords | TOXIN / insecticidal / pore forming / protoxin | ||||||
Function / homology | Function and homology information symbiont-mediated killing of host cell / sporulation resulting in formation of a cellular spore / toxin activity / signaling receptor binding Similarity search - Function | ||||||
Biological species | Bacillus thuringiensis serovar kurstaki str. HD73 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.78 Å | ||||||
Authors | Evdokimov, A.G. / Moshiri, F. / Sturman, E.J. / Rydel, T.J. / Zheng, M. / Seale, J.W. / Franklin, S. | ||||||
Citation | Journal: Protein Sci. / Year: 2014 Title: Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals. Authors: Evdokimov, A.G. / Moshiri, F. / Sturman, E.J. / Rydel, T.J. / Zheng, M. / Seale, J.W. / Franklin, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4w8j.cif.gz | 217.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4w8j.ent.gz | 168.7 KB | Display | PDB format |
PDBx/mmJSON format | 4w8j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w8/4w8j ftp://data.pdbj.org/pub/pdb/validation_reports/w8/4w8j | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 133981.031 Da / Num. of mol.: 1 Mutation: C661S,C730S,C796S,C802S,C814S,C816S,C822S,C837S,C990S,C1025S,C1045S,C1063S,C1076S,C1125S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus thuringiensis serovar kurstaki str. HD73 (bacteria) Gene: HD73_6004 / Plasmid: pCry1Ac Details (production host): sporulation promoter, chloramphenicol resistance Production host: Bacillus thuringiensis (bacteria) / Strain (production host): EG10650 / References: UniProt: M4LET9, UniProt: P05068*PLUS | ||||
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#2: Chemical | #3: Chemical | ChemComp-CA / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.89 Å3/Da / Density % sol: 35.09 % / Description: tetragonal bipyramid |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 7.84 Details: 600 nL of 13 mg/mL protein in 20 mM ethanolamine buffer with 0.35 M NaCl was mixed with 600 nL of 700 mM sodium-potassium tartrate, 100 mM BIS-TRIS propane pH 7.84 and 120 nL of 9 mM n-decyl ...Details: 600 nL of 13 mg/mL protein in 20 mM ethanolamine buffer with 0.35 M NaCl was mixed with 600 nL of 700 mM sodium-potassium tartrate, 100 mM BIS-TRIS propane pH 7.84 and 120 nL of 9 mM n-decyl thiomaltoside, and the resulting 1.2 uL sitting drop was allowed to equili- brate against 80uL of the tartrate/BIS-TRIS propane reservoir solution at 19C. PH range: 7.8-7.9 |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
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Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 2, 2011 |
Radiation | Monochromator: Si-111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.78→87 Å / Num. obs: 26818 / % possible obs: 99.6 % / Redundancy: 4.6 % / Rmerge(I) obs: 0.096 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 2.78→2.9 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 2.1 / % possible all: 100 |
-Processing
Software | Name: REFMAC / Version: 5.5.0109 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: in house Resolution: 2.78→82.97 Å / Cor.coef. Fo:Fc: 0.926 / Cor.coef. Fo:Fc free: 0.85 / SU B: 18.927 / SU ML: 0.387 / Cross valid method: THROUGHOUT / ESU R Free: 0.539 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 53.344 Å2
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Refinement step | Cycle: 1 / Resolution: 2.78→82.97 Å
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Refine LS restraints |
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