5MRS
Crystal structure of L1 protease Lysobacter sp. XL1 in complex with AEBSF
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 | 2015-07-10 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.96863 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.855, 122.553, 78.988 |
| Unit cell angles | 90.00, 98.64, 90.00 |
Refinement procedure
| Resolution | 48.207 - 1.900 |
| R-factor | 0.2026 |
| Rwork | 0.201 |
| R-free | 0.24190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5mrr |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.881 |
| 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 | 1.970 |
| High resolution limit [Å] | 1.860 | 1.860 |
| Number of reflections | 65564 | |
| <I/σ(I)> | 8.13 | 1.7 |
| Completeness [%] | 99.4 | 99.5 |
| Redundancy | 4.75 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 1,4M Lithium sulphate, 0,1M BisTris, |
