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 |