+Open data
-Basic information
Entry | Database: PDB / ID: 3gt6 | ||||||
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Title | Crystal Structure of the hspA from Xanthomonas axonopodis | ||||||
Components | Low molecular weight heat shock protein | ||||||
Keywords | CHAPERONE / hspA / shp / shsp / Xanthomonas axonopodis / high resolution / stress response | ||||||
Function / homology | Function and homology information : / Immunoglobulin-like - #790 / Hsp20/alpha crystallin family / Small heat shock protein (sHSP) domain profile. / Alpha crystallin/Hsp20 domain / HSP20-like chaperone / Immunoglobulin-like / Sandwich / Mainly Beta Similarity search - Domain/homology | ||||||
Biological species | Xanthomonas axonopodis pv. citri (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.15 Å | ||||||
Authors | Hilario, E. / Medrano, F.J. / Bertolini, M.C. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2011 Title: Crystal structures of Xanthomonas small heat shock protein provide a structural basis for an active molecular chaperone oligomer. Authors: Hilario, E. / Martin, F.J. / Bertolini, M.C. / Fan, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3gt6.cif.gz | 55.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3gt6.ent.gz | 40.2 KB | Display | PDB format |
PDBx/mmJSON format | 3gt6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gt/3gt6 ftp://data.pdbj.org/pub/pdb/validation_reports/gt/3gt6 | HTTPS FTP |
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-Related structure data
Related structure data | 3gufC 3glaS 3gtb S: Starting model for refinement C: citing same article (ref.) |
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Similar 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: 11610.074 Da / Num. of mol.: 2 / Fragment: UNP residues 37-139 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xanthomonas axonopodis pv. citri (bacteria) Gene: hspA / Plasmid: pET28a-hspA / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q8PNC2 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.79 Å3/Da / Density % sol: 67.53 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 24% (w/v) PEG 1500, 20 % glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 293 K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: LNLS / Beamline: D03B-MX1 / Wavelength: 1.43 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Jan 24, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.43 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→26.96 Å / Num. obs: 18680 / Redundancy: 3.8 % / Rmerge(I) obs: 0.049 |
-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR | Rfactor: 28.34 / Model details: Phaser MODE: MR_AUTO
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3GLA Resolution: 2.15→26.96 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.917 / WRfactor Rfree: 0.234 / WRfactor Rwork: 0.196 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.855 / SU B: 3.865 / SU ML: 0.103 / SU R Cruickshank DPI: 0.175 / SU Rfree: 0.162 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.175 / ESU R Free: 0.162 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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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 max: 60.93 Å2 / Biso mean: 26.304 Å2 / Biso min: 10.63 Å2
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Refinement step | Cycle: LAST / Resolution: 2.15→26.96 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.201 Å / Total num. of bins used: 20
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