5MRR
Crystal structure of L1 protease of Lysobacter sp. XL1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-05-16 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97625 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 63.710, 96.480, 118.180 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.985 - 1.350 |
| R-factor | 0.1586 |
| Rwork | 0.157 |
| R-free | 0.19040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2alp |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.851 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.340 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Number of reflections | 199062 | |
| <I/σ(I)> | 8.9 | 1.4 |
| Completeness [%] | 99.1 | 98 |
| Redundancy | 4.98 | 4.98 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 1,4M Lithium sulphate, 0,1M BisTris |
