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3MQP

Crystal Structure of human BFL-1 in complex with NOXA BH3 peptide, Northeast Structural Genomics Consortium Target HR2930

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X29A
Synchrotron siteNSLS
BeamlineX29A
Temperature [K]100
Detector technologyCCD
Collection date2010-04-23
DetectorADSC QUANTUM 315r
Wavelength(s)1.075
Spacegroup nameP 1 21 1
Unit cell lengths43.138, 43.196, 46.387
Unit cell angles90.00, 113.50, 90.00
Refinement procedure
Resolution30.300 - 2.240
R-factor0.182
Rwork0.177
R-free0.23000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3i1h
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwarePHASER
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.3002.330
High resolution limit [Å]2.2402.250
Rmerge0.0930.383
Number of reflections7385
<I/σ(I)>3.06
Completeness [%]97.784.6
Redundancy5.94.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.4296Protein solution: 100mM NaCl, 5mM DTT, 0.02% NaN3, 10mM Tris-HCl (pH 7.5) . Reservoir solution: 1.5 M Sodium Malonate, 0.1 M sodium Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 296K

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