7RGV
Structure of Caulobacter crescentus Suppressor of copper sensitivity protein C
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 | PIXEL |
Collection date | 2021-02-21 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9536 |
Spacegroup name | P 63 |
Unit cell lengths | 113.948, 113.948, 48.695 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 49.340 - 2.630 |
R-factor | 0.2263 |
Rwork | 0.224 |
R-free | 0.25020 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4VXW res 50-224 chain A |
RMSD bond length | 0.002 |
RMSD bond angle | 0.446 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.19_4092) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.340 | 2.740 |
High resolution limit [Å] | 2.630 | 2.630 |
Rmerge | 0.052 | 1.460 |
Rmeas | 0.054 | 1.520 |
Rpim | 0.016 | 0.431 |
Number of reflections | 10854 | 1045 |
<I/σ(I)> | 22.51 | 1.85 |
Completeness [%] | 98.8 | 94.76 |
Redundancy | 12 | 12.3 |
CC(1/2) | 1.000 | 0.961 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.25 | 277.15 | Protein reduced with DTT and purified in 25 mM HEPES pH 7.5, 150 mM NaCl. Protein concentrated to 130 mg/ml. 1ul of protein solution mixed with 1ul of crystallant solution: 39% MPD, 200 mM NaAcetate, 20 mM CaCl2 pH 7.25 |