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3RFI

Crystal structure of the saposin-like domain of plant aspartic protease from Solanum tuberosum

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsOTHER
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2009-11-09
DetectorMAR scanner 345 mm plate
Wavelength(s)1.5418
Spacegroup nameP 32 2 1
Unit cell lengths56.470, 56.470, 55.340
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution25.000 - 1.900
R-factor0.18995
Rwork0.187
R-free0.24980
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.020
RMSD bond angle1.808
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwarePHASER
Refinement softwareREFMAC (5.5.0104)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]40.0002.000
High resolution limit [Å]1.9001.900
Rmerge0.0590.900
Number of reflections8355
<I/σ(I)>24.12.87
Completeness [%]99.9100
Redundancy10.310.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP2930.2M Lithium sulfate monohydrate, 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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