3WG5
1510-N membrane-bound stomatin-specific protease K138A mutant in complex with a substrate peptide under heat treatment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-19 |
| Detector | RIGAKU SATURN A200 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 111.448, 111.448, 91.738 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.400 |
| R-factor | 0.20554 |
| Rwork | 0.202 |
| R-free | 0.24082 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3viv |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.171 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0044) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.049 | 0.325 |
| Number of reflections | 23169 | |
| <I/σ(I)> | 61.9 | 7.8 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 9.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 0.8M imidazole, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
