6OFT
The crystal structure of the first half of the periplasmic protease PqqL from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-03-08 |
| Detector | MAR CCD 130 mm |
| Wavelength(s) | 0.987 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 71.070, 84.440, 92.070 |
| Unit cell angles | 90.00, 102.24, 90.00 |
Refinement procedure
| Resolution | 21.360 - 2.000 |
| R-factor | 0.194 |
| Rwork | 0.193 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3amj |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.020 |
| 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] | 21.360 | 2.040 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.348 | 2.009 |
| Rpim | 0.070 | 0.531 |
| Number of reflections | 71853 | 4575 |
| <I/σ(I)> | 14.4 | 1.7 |
| Completeness [%] | 99.8 | 99 |
| Redundancy | 22.3 | 15.1 |
| CC(1/2) | 0.998 | 0.610 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 4.2 | 293 | 0.1 M phosphate-citrate buffer, 0.2 M NaCl, 20% PEG 8000 |
