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2Q2I

Crystal structure of the protein secretion chaperone CsaA from Agrobacterium tumefaciens.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2004-08-24
DetectorRIGAKU RAXIS IV
Wavelength(s)1.54
Spacegroup nameP 61
Unit cell lengths60.653, 60.653, 113.389
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution52.530 - 1.550
R-factor0.18
Rwork0.178
R-free0.20800
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1gd7
RMSD bond length0.010
RMSD bond angle1.282
Data reduction softwareCrystalClear
Data scaling softwared*TREK (8.0SSI)
Phasing softwarePHASER
Refinement softwareREFMAC (5.2.0005)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]52.5301.610
High resolution limit [Å]1.5501.550
Rmerge0.0400.341
Total number of observations35222
Number of reflections34123
<I/σ(I)>23.77.2
Completeness [%]99.899.6
Redundancy10.8210.13
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.52941.8M ammonium sulfate, 0.1M HEPES pH 7.5, 2% PEG400, 5% ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 294K

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