4P3V
Crystal structure of the E. coli HU beta2 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-02-03 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.98401 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 51.107, 51.107, 110.462 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.260 - 1.250 |
| R-factor | 0.1565 |
| Rwork | 0.156 |
| R-free | 0.17340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mul |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.888 |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.260 | 1.270 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmerge | 0.045 | 0.892 |
| Number of reflections | 24255 | |
| <I/σ(I)> | 20.9 | 2.1 |
| Completeness [%] | 99.4 | 97.9 |
| Redundancy | 9.4 | 8.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 293 | 30% PEG800, 0.2M lithium sulfate, 0.1M sodium acetate |






