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Crystal structure of the autoproteolytic domain from the nuclear pore complex component NUP145 from Saccharomyces cerevisiae in the Hexagonal, P61 space group

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 31-ID
Synchrotron siteAPS
Beamline31-ID
Temperature [K]100
Detector technologyCCD
Collection date2009-08-02
DetectorRAYONIX MX225HE
Wavelength(s)0.97929
Spacegroup nameP 61
Unit cell lengths135.052, 135.052, 56.154
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution25.520 - 2.100
R-factor0.192
Rwork0.190
R-free0.23000
Structure solution methodSAD
RMSD bond length0.019
RMSD bond angle1.494
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareSHELX (C)
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.9202.210
High resolution limit [Å]2.1002.100
Number of reflections34126
<I/σ(I)>21.28.2
Completeness [%]99.299
Redundancy21.719.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP2941600mM tri-sodium citrate dehydrate, VAPOR DIFFUSION, SITTING DROP, temperature 294K

246031

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