5NZW
Crystal structure of DNA cross-link repair protein 1A in complex with ceftriaxone
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 | 2016-11-26 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.972 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.356, 58.495, 112.538 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.500 - 2.700 |
R-factor | 0.23056 |
Rwork | 0.226 |
R-free | 0.31504 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5aho |
RMSD bond length | 0.010 |
RMSD bond angle | 1.453 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.500 | 2.830 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.100 | 1.700 |
Rpim | 0.785 | |
Number of reflections | 9762 | 1255 |
<I/σ(I)> | 10.1 | 1.3 |
Completeness [%] | 99.6 | 99.9 |
Redundancy | 6.2 | 6.7 |
CC(1/2) | 0.999 | 0.460 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 278 | 30% PEG 1000, 0.1 M MIB buffer pH 6.0 |