7YWP
Closed conformation of Oligopeptidase B from Serratia proteomaculans with covalently bound TCK
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-05-31 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.529, 89.660, 108.650 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.310 - 2.200 |
| R-factor | 0.1879 |
| Rwork | 0.184 |
| R-free | 0.25440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7ob1 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.566 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.078 | 0.190 |
| Rmeas | 0.090 | 0.270 |
| Number of reflections | 37524 | 5487 |
| <I/σ(I)> | 6.6952 | 3.89 |
| Completeness [%] | 98.6 | 99.9 |
| Redundancy | 4.14 | 4.27 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 200 mM Lithium sulfate, 100 mM Bis-Tris pH 5.5, 23% PEG 3350 |
