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1E6O

Crystal structure of Fab13B5 against HIV-1 capsid protein p24

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1997-04-15
DetectorMARRESEARCH
Spacegroup nameP 21 21 21
Unit cell lengths36.680, 81.900, 134.400
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000 - 1.800
R-factor0.225
Rwork0.225
R-free0.25500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1afv
RMSD bond length0.005
RMSD bond angle1.400
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareX-PLOR (3.8)
Refinement softwareX-PLOR (3.8)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0001.850
High resolution limit [Å]1.8001.800
Rmerge0.063

*

0.128

*

Total number of observations124392

*

Number of reflections35964
Completeness [%]94.085.5

*

Redundancy3.53.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.822

*

7MG/ML OF FAB'13B5 IN 0.1M PIPES PH=7.8 IN 9% TO 11% PEG8000 AFTER EQUILIBRATION IN HANGING DROPS AT 22C, pH 7.80
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG80009-11 (%)
21reservoirPIPES0.1 (M)

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