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4FRU

Crystal structure of horse wild-type cyclophilin B

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 4.2.2
Synchrotron siteALS
Beamline4.2.2
Temperature [K]100
Detector technologyCCD
Collection date2010-08-12
DetectorNOIR-1
Wavelength(s)0.827
Spacegroup nameC 1 2 1
Unit cell lengths64.880, 44.070, 60.570
Unit cell angles90.00, 95.20, 90.00
Refinement procedure
Resolution16.416 - 1.100
R-factor0.1167
Rwork0.116
R-free0.13910
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1cyn
RMSD bond length0.007
RMSD bond angle1.301
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwarePHENIX ((phenix.refine: 1.8_1069))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]16.4201.160
High resolution limit [Å]1.1001.100
Rmerge0.0780.272
Number of reflections62397
<I/σ(I)>9.83.9
Completeness [%]90.453.4
Redundancy3.32
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.22950.1M MES, 10mM ZnCl2, 10% glycerol, 28% PEG MME 550, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K

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