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6F2H

Structure of Protease 1 from Pyrococcus horikoshii co-crystallized in presence of 10 mM Tb-Xo4 and potassium iodide.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM30A
Synchrotron siteESRF
BeamlineBM30A
Temperature [K]100
Detector technologyCCD
Collection date2015-10-08
DetectorADSC QUANTUM 315r
Wavelength(s)1.6492
Spacegroup nameP 1 21 1
Unit cell lengths82.577, 84.698, 144.343
Unit cell angles90.00, 90.97, 90.00
Refinement procedure
Resolution46.010 - 2.190
R-factor0.152
Rwork0.150
R-free0.19300
RMSD bond length0.010
RMSD bond angle0.910
Data reduction softwareXDS
Data scaling softwareSCALA
Phasing softwareautoSHARP
Refinement softwareBUSTER (2.10.3)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]46.010
High resolution limit [Å]2.1902.190
Rpim0.0720.447
Number of reflections101279
<I/σ(I)>11.43
Completeness [%]99.1
Redundancy6.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP293100 mM Bis tris propane pH 7, 20 to 30% PEG3350, Potassium Iodide 200 mM. Tb-Xo4 was directly mixed with the protein solution at a final concentration of 10 mM prior to crystallization.

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