5T88
Prolyl oligopeptidase from Pyrococcus furiosus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-04-23 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.535, 176.757, 57.901 |
Unit cell angles | 90.00, 106.03, 90.00 |
Refinement procedure
Resolution | 47.092 - 1.902 |
R-factor | 0.1942 |
Rwork | 0.193 |
R-free | 0.24730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bkl |
RMSD bond length | 0.013 |
RMSD bond angle | 1.435 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.175 | |
Number of reflections | 83502 | |
<I/σ(I)> | 12.3 | 1.5 |
Completeness [%] | 99.9 | 100 |
Redundancy | 9.7 | 9.3 |
CC(1/2) | 0.575 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 298 | 30% w/w PEG 8000 100 mM Tris pH 9.0 |