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5EUF

The crystal structure of a protease from Helicobacter pylori

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyCCD
Collection date2014-12-05
DetectorADSC QUANTUM 315r
Wavelength(s)0.97918, 0.97940
Spacegroup nameC 1 2 1
Unit cell lengths155.159, 50.266, 147.889
Unit cell angles90.00, 94.86, 90.00
Refinement procedure
Resolution47.803 - 2.800
R-factor0.1894
Rwork0.186
R-free0.24450
Structure solution methodMAD
RMSD bond length0.002
RMSD bond angle0.598
Data reduction softwareHKL-3000
Data scaling softwareHKL-3000
Phasing softwareHKL-3000
Refinement softwarePHENIX (1.9_1692)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]48.0002.850
High resolution limit [Å]2.8002.800
Rmerge0.1240.701
Number of reflections27514
<I/σ(I)>91.6
Completeness [%]95.392.1
Redundancy3.73
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.52890.2M Calcium Acetate, 0.1M HEPES:NaOH, 10% (w/v) PEG8000

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