4ZOQ
Crystal Structure of a Lanthipeptide Protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-08-03 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 |
| Unit cell lengths | 71.040, 112.780, 114.770 |
| Unit cell angles | 82.17, 89.68, 82.85 |
Refinement procedure
| Resolution | 38.031 - 2.350 |
| R-factor | 0.202 |
| Rwork | 0.200 |
| R-free | 0.24960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.544 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.5.1) |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.450 |
| High resolution limit [Å] | 2.350 | 10.000 | 2.350 |
| Rmerge | 0.085 | 0.022 | 0.885 |
| Rmeas | 0.098 | 0.026 | 1.023 |
| Total number of observations | 568612 | ||
| Number of reflections | 143709 | 1833 | 16843 |
| <I/σ(I)> | 13.14 | 46.31 | 1.73 |
| Completeness [%] | 98.5 | 98.1 | 97.8 |
| Redundancy | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | Precipitant of 20% PEG 3350, 2% tacsimate pH=7.0 and 4 mM HEPES pH=6.8 |
