8ONO
Modified oligopeptidase B from S. proteamaculans in intermediate conformation with 5 spermine molecule at 1.65 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-10-10 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 73.090, 100.620, 108.630 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.590 - 1.650 |
| R-factor | 0.18778 |
| Rwork | 0.186 |
| R-free | 0.21980 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.795 |
| 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 | 1.740 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.050 | 0.330 |
| Rmeas | 0.056 | 0.359 |
| Number of reflections | 95311 | 13658 |
| <I/σ(I)> | 9.2633 | 2.29 |
| Completeness [%] | 98.6 | |
| Redundancy | 5.84 |
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 |
