5MAV
Crystal structure of human PCNA in complex with PARG (poly(ADP-ribose) glycohydrolase) peptide.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-06-29 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.968 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 77.597, 153.604, 85.512 |
| Unit cell angles | 90.00, 96.90, 90.00 |
Refinement procedure
| Resolution | 47.671 - 2.575 |
| R-factor | 0.2412 |
| Rwork | 0.239 |
| R-free | 0.29090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vym |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.041 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 47.671 |
| High resolution limit [Å] | 2.570 |
| Rmerge | 0.260 |
| Rmeas | 0.293 |
| Rpim | 0.132 |
| Number of reflections | 62473 |
| <I/σ(I)> | 5.6 |
| Completeness [%] | 99.1 |
| Redundancy | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295.15 | 0.1 M Tris-HCl pH 7.5, 20% PEG 3350, 0.2 M ammonium acetate |
