6HK5
X-ray structure of a truncated mutant of the metallochaperone CooJ with a high-affinity nickel-binding site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID30B |
Synchrotron site | ESRF |
Beamline | ID30B |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-11-12 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.97856 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.800, 74.280, 70.640 |
Unit cell angles | 90.00, 92.74, 90.00 |
Refinement procedure
Resolution | 46.746 - 2.042 |
R-factor | 0.2024 |
Rwork | 0.200 |
R-free | 0.25850 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.000 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SHELXD |
Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.746 | 2.160 |
High resolution limit [Å] | 2.040 | 2.040 |
Rmeas | 0.140 | 0.880 |
Number of reflections | 30586 | 4749 |
<I/σ(I)> | 9.4 | 1.63 |
Completeness [%] | 99.2 | 96 |
Redundancy | 6.4 | 6.2 |
CC(1/2) | 0.997 | 0.691 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 294 | protein concentration of 10 mgmL-1 and 1 equivalent of Ni(II) per dimer, crystals were grown in 16% PEG3350 and 0.2 M calcium chloride |