6PYM
Structure of active-site serine mutant of ESP, serine protease from Staphylococcus epidermidis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2018-07-07 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.621, 61.026, 42.512 |
| Unit cell angles | 90.00, 98.66, 90.00 |
Refinement procedure
| Resolution | 39.169 - 1.200 |
| R-factor | 0.158801782518 |
| Rwork | 0.159 |
| R-free | 0.16462 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4jcn |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.825 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.169 | 1.243 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.015 | |
| Rmeas | 0.022 | |
| Number of reflections | 119842 | 5576 |
| <I/σ(I)> | 30.81 | |
| Completeness [%] | 97.0 | 89 |
| Redundancy | 2 | 2 |
| CC(1/2) | 0.998 | 0.995 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 20% PEG 8000, 0.1M HEPES, pH 7.5 |
