5EKA
HU DNA-binding protein from Thermus thermophilus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2) |
| Synchrotron site | PETRA III, EMBL c/o DESY |
| Beamline | P14 (MX2) |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-04-26 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97631 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 55.464, 38.432, 44.861 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.860 - 1.690 |
| R-factor | 0.20077 |
| Rwork | 0.198 |
| R-free | 0.25612 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1b8z |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.477 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.900 | 1.740 |
| High resolution limit [Å] | 1.690 | 1.690 |
| Rmerge | 0.073 | 0.510 |
| Number of reflections | 10742 | |
| <I/σ(I)> | 22.6 | 3 |
| Completeness [%] | 96.3 | 59.6 |
| Redundancy | 12 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.3 | 293 | Protein solutions of 14-18 mg/ml, Buffer: 0.2 M Na-formate, Precipitating agent: 20%(w/v) PEG 3350 |
