8AF1
Beta-Lytic Protease from Lysobacter capsici
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-02-25 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.003185 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 70.580, 44.130, 52.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.230 - 1.570 |
| R-factor | 0.1538 |
| Rwork | 0.151 |
| R-free | 0.20290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3it5 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.871 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 1.610 |
| High resolution limit [Å] | 1.570 | 1.570 |
| Rmeas | 0.190 | 1.160 |
| Number of reflections | 23631 | 1701 |
| <I/σ(I)> | 11.16 | 2.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 12.5 | 12.5 |
| CC(1/2) | 0.990 | 0.690 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 297 | 400 mM NaCl, 30 mM Na-acetate |
