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1VQ0

Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL9-1
Synchrotron siteSSRL
BeamlineBL9-1
Temperature [K]100
Detector technologyCCD
Collection date2004-04-08
DetectorADSC QUANTUM 315
Spacegroup nameP 21 21 21
Unit cell lengths76.213, 101.673, 113.686
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution49.620 - 2.200
R-factor0.20033
Rwork0.198
R-free0.24079
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1i7f
RMSD bond length0.019
RMSD bond angle1.588
Data reduction softwareMOSFLM
Data scaling softwareSCALA (4.2))
Phasing softwareMOLREP
Refinement softwareREFMAC (5.1.9999)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]49.6202.260
High resolution limit [Å]2.2002.200
Number of reflections44233
<I/σ(I)>10.72.2
Completeness [%]97.486.9
Redundancy3.52.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION,SITTING DROP,NANODROP7.527715.0% Glycerol, 8.5% iso-Propanol, 17.0% PEG-4000, 0.1M HEPES pH 7.5, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K

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