2V1U
STRUCTURE OF THE AEROPYRUM PERNIX ORC1 PROTEIN IN COMPLEX WITH DNA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 200 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 75.700, 75.700, 395.110 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 3.100 |
| R-factor | 0.257 |
| Rwork | 0.254 |
| R-free | 0.29700 |
| Structure solution method | MAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.003 |
| RMSD bond angle | 1.147 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 3.200 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.060 | 0.250 |
| Number of reflections | 12348 | |
| <I/σ(I)> | 15.41 | 4.52 |
| Completeness [%] | 99.3 | 99.3 |
| Redundancy | 5 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | pH 6.5 |
