6DRT
Crystal structure of the processivity clamp GP45 complexed with recognition peptide of ligase from bacteriophage T4
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-26 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 63.757, 90.950, 151.403 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.783 - 2.117 |
| R-factor | 0.2009 |
| Rwork | 0.199 |
| R-free | 0.24030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1czd |
| RMSD bond length | 0.001 |
| RMSD bond angle | 0.368 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.14rc1_3161) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 63.760 | 2.230 |
| High resolution limit [Å] | 2.117 | 2.117 |
| Rmerge | 0.061 | 1.340 |
| Number of reflections | 50401 | 4893 |
| <I/σ(I)> | 15.7 | 1.2 |
| Completeness [%] | 99.1 | 98.8 |
| Redundancy | 2.6 | 5.1 |
| CC(1/2) | 0.999 | 0.562 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | PEG3350 |






