2VTX
ACTIVATION OF NUCLEOPLASMIN, AN OLIGOMERIC HISTONE CHAPERONE, CHALLENGES ITS STABILITY
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 67.034, 94.601, 176.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.500 |
| R-factor | 0.187 |
| Rwork | 0.182 |
| R-free | 0.26900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k5j |
| RMSD bond length | 0.034 |
| RMSD bond angle | 2.483 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.070 | 0.310 |
| Number of reflections | 57758 | |
| <I/σ(I)> | 7.7 | 17.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | 15 MG/ML PROTEIN, 100MM NAAC, 20MM CACL2, 30% MPD, pH 4.6 |
