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3H13

c-FLIPL protease-like domain

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X29A
Synchrotron siteNSLS
BeamlineX29A
Temperature [K]100
Detector technologyCCD
Collection date2007-04-09
DetectorADSC QUANTUM 315
Wavelength(s)1.1
Spacegroup nameP 31 2 1
Unit cell lengths101.940, 101.940, 61.360
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution29.430 - 2.200
R-factor0.187
Rwork0.187
R-free0.22000
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.012
RMSD bond angle1.500
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwareCNS (1.2)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]100.0002.280
High resolution limit [Å]2.2002.200
Number of reflections19006
<I/σ(I)>19.46.8
Completeness [%]99.9100
Redundancy6.46.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.52900.1 M Mes, 18% PEG, 5000 monomethyl ether, 0.1 M ammonium sulfate , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K

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