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 |
