1XE0
The structure and function of Xenopus NO38-core, a histone binding chaperone in the nucleolus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-01-14 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54 |
Spacegroup name | P 1 |
Unit cell lengths | 59.000, 59.000, 87.200 |
Unit cell angles | 77.00, 88.30, 60.90 |
Refinement procedure
Resolution | 84.520 - 1.700 |
R-factor | 0.21239 |
Rwork | 0.208 |
R-free | 0.25908 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1xb9 |
RMSD bond length | 0.029 |
RMSD bond angle | 2.439 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 90.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.030 | 0.182 |
Number of reflections | 109907 | |
<I/σ(I)> | 9.6 | 4.2 |
Completeness [%] | 79.7 | 88.2 |
Redundancy | 4.5 | 13.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 296 | PEG400, Ethylene glycol, Tris-HCl, Magnesium Chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K |