5TSA
Crystal structure of the Zrt-/Irt-like protein from Bordetella bronchiseptica with bound Zn2+
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 193 |
Detector technology | PIXEL |
Collection date | 2016-10-21 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.2782 |
Spacegroup name | I 1 2 1 |
Unit cell lengths | 55.006, 61.073, 94.394 |
Unit cell angles | 90.00, 104.02, 90.00 |
Refinement procedure
Resolution | 33.373 - 2.400 |
R-factor | 0.2143 |
Rwork | 0.212 |
R-free | 0.25710 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | TBA |
RMSD bond length | 0.008 |
RMSD bond angle | 0.965 |
Data scaling software | Aimless (0.5.28) |
Phasing software | PHASER (2.6.0) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 33.373 | 41.910 | 2.490 |
High resolution limit [Å] | 2.400 | 8.960 | 2.400 |
Rmerge | 0.116 | 0.055 | 0.829 |
Rmeas | 0.125 | ||
Rpim | 0.048 | ||
Total number of observations | 80183 | ||
Number of reflections | 11734 | ||
<I/σ(I)> | 11.7 | ||
Completeness [%] | 97.5 | 97.6 | 93.6 |
Redundancy | 6.8 | 6.2 | 7 |
CC(1/2) | 0.998 | 0.998 | 0.819 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | LIPIDIC CUBIC PHASE | 7.5 | 294 | protein concentration: 15 mg/mL; buffer: 10 mM Hepes pH 7.3, 300 mM NaCl, 5% Glycerol, 0.02% DDM; crystallization condition: 0.1 M Sodium chloride, 0.1 M Cadmium chloride hemi, 0.1 M Tris-HCl pH 7.5, 33% PEG 400 |