6DCR
E. coli PriA helicase winged helix domain deletion protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-11-26 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 1.12712 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.132, 56.505, 195.863 |
| Unit cell angles | 90.00, 97.67, 90.00 |
Refinement procedure
| Resolution | 48.832 - 1.978 |
| R-factor | 0.1871 |
| Rwork | 0.186 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4NL4 removing the winged helix domain |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.177 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.832 | 2.049 |
| High resolution limit [Å] | 1.978 | 1.978 |
| Rmerge | 0.059 | 1.299 |
| Rmeas | 0.069 | 1.513 |
| Rpim | 0.036 | 0.766 |
| Number of reflections | 101849 | 9857 |
| <I/σ(I)> | 11.18 | 1.03 |
| Completeness [%] | 96.8 | 94.98 |
| Redundancy | 3.7 | 3.7 |
| CC(1/2) | 0.998 | 0.374 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 297 | 50 mM HEPES-HCl pH 7.5, 9.5 % PEG 4000, 4 % Isopropanol, 8 % glycerol, 50 mM sodium malonate, and 25-100 mM sodium fluoride |
