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3KEP

Crystal structure of the autoproteolytic domain from the nuclear pore complex component NUP145 from Saccharomyces cerevisiae

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 31-ID
Synchrotron siteAPS
Beamline31-ID
Temperature [K]100
Detector technologyCCD
Collection date2009-08-01
DetectorRAYONIX MX225HE
Wavelength(s)0.97929
Spacegroup nameP 43 21 2
Unit cell lengths91.037, 91.037, 108.394
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution27.670 - 1.820
R-factor0.214
Rwork0.213
R-free0.24400
Structure solution methodSAD
RMSD bond length0.020
RMSD bond angle1.662
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareSHELX (C)
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.7801.920
High resolution limit [Å]1.8201.820
Number of reflections41497
<I/σ(I)>22.98.8
Completeness [%]99.9100
Redundancy29.129.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.5294100mM HEPES, 25% PEG 3350, 200mM NaCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K

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