6OFS
The crystal structure of the periplasmic protease PqqL from Escherichia coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-03-08 |
Detector | MAR CCD 130 mm |
Wavelength(s) | 0.987 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 98.674, 98.674, 230.814 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.130 - 2.600 |
R-factor | 0.201 |
Rwork | 0.199 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | TBA |
RMSD bond length | 0.009 |
RMSD bond angle | 1.080 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | BUSTER (2.10.3) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.250 | 2.720 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.354 | 6.338 |
Rpim | 0.044 | 0.645 |
Number of reflections | 36058 | 4290 |
<I/σ(I)> | 25.1 | 1.6 |
Completeness [%] | 100.0 | 100 |
Redundancy | 125.2 | 96.9 |
CC(1/2) | 0.999 | 0.542 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 8.5 | 293 | 0.1 M Bis-tris propane, 0.2 M NaK tartrate, 20 % PEG 3350 |