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 |