3VIV
1510-N membrane-bound stomatin-specific protease K138A mutant in complex with a substrate peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE AR-NW12A |
| Synchrotron site | Photon Factory |
| Beamline | AR-NW12A |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2010-12-19 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 111.473, 111.473, 91.768 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.740 - 2.250 |
| R-factor | 0.2157 |
| Rwork | 0.212 |
| R-free | 0.24760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bpp |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.338 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.330 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.054 | 0.341 |
| Number of reflections | 27554 | |
| <I/σ(I)> | 67.9 | 9.8 |
| Completeness [%] | 98.7 | 100 |
| Redundancy | 10.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 1.0M imidazole, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
