5MS7
Crystal structure of the legionella pneumophila effector protein RavZ_20-502
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 | 2016-02-26 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.97862 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 222.770, 222.770, 72.940 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.145 - 2.800 |
R-factor | 0.2091 |
Rwork | 0.207 |
R-free | 0.25350 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5cqc |
RMSD bond length | 0.009 |
RMSD bond angle | 1.379 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.150 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.194 | 1.951 |
Number of reflections | 22921 | |
<I/σ(I)> | 15.14 | 1.94 |
Completeness [%] | 100.0 | 100 |
Redundancy | 26.7 | 26.3 |
CC(1/2) | 0.999 | 0.165 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 277.15 | 16% PEG3350, 0.2 M BaCl2 and 0.1 M MES |