6MDW
Mechanism of protease dependent DPC repair
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-10-13 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9792 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 128.422, 29.553, 50.242 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.580 - 1.500 |
R-factor | 0.16497 |
Rwork | 0.163 |
R-free | 0.19314 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6mdx |
RMSD bond length | 0.008 |
RMSD bond angle | 1.401 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Rpim | 0.024 | 0.253 |
Number of reflections | 31618 | 1531 |
<I/σ(I)> | 30.47 | |
Completeness [%] | 99.4 | |
Redundancy | 10.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293.15 | 0.1 M sodium citrate tribasic dihydrate at pH 5.5, 14% (w/v) PEG8000, and 10 mM ATP |