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 |