5DA7
monomeric PCNA bound to a small protein inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-09-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.075 |
| Spacegroup name | F 2 2 2 |
| Unit cell lengths | 82.341, 184.079, 330.684 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.962 - 2.802 |
| R-factor | 0.2035 |
| Rwork | 0.201 |
| R-free | 0.26110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lx1 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.360 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.116 | 0.892 |
| Number of reflections | 30707 | |
| <I/σ(I)> | 36.6 | |
| Completeness [%] | 98.9 | |
| Redundancy | 19.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 298 | Well solution: 1.2 M ammonium sulfate, 50 mM sodium citrate buffer, and 10% glycerol |
