4NSY
Wild-type lysobacter enzymogenes lysc endoproteinase covalently inhibited by TLCK
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-11-04 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.579, 135.810, 45.587 |
| Unit cell angles | 90.00, 97.19, 90.00 |
Refinement procedure
| Resolution | 33.993 - 1.100 |
| R-factor | 0.1662 |
| Rwork | 0.164 |
| R-free | 0.20820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1arb |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.198 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: dev_1520)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.600 | 1.140 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.107 | 0.952 |
| Number of reflections | 182416 | |
| <I/σ(I)> | 6.2978 | 1.0009 |
| Completeness [%] | 95.5 | 83.4 |
| Redundancy | 3.3 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 0.2M CaCl2, 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
