4NSV
Lysobacter enzymogenes lysc endoproteinase K30R mutant 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 | 2013-08-13 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.7 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.605, 135.582, 45.553 |
| Unit cell angles | 90.00, 98.01, 90.00 |
Refinement procedure
| Resolution | 39.218 - 0.900 |
| R-factor | 0.1391 |
| Rwork | 0.138 |
| R-free | 0.15790 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1arb |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.399 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: dev_1539)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.800 | 0.930 |
| High resolution limit [Å] | 0.900 | 0.900 |
| Rmerge | 0.076 | 0.011 |
| Number of reflections | 339560 | |
| <I/σ(I)> | 8.6924 | 1.0521 |
| Completeness [%] | 97.5 | 95 |
| Redundancy | 3.4 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 293 | 0.1M Tris/HCl pH 8.5, 0.2M Li2SO4, 25% PEG 3350, temperature 293K |
