3GFC
Crystal Structure of Histone-binding protein RBBP4
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E DW |
Temperature [K] | 100 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.645, 87.214, 88.203 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.300 |
R-factor | 0.217 |
Rwork | 0.214 |
R-free | 0.26100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3cfs |
RMSD bond length | 0.017 |
RMSD bond angle | 1.721 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 88.040 | 50.000 | 2.380 |
High resolution limit [Å] | 2.300 | 4.950 | 2.300 |
Rmerge | 0.090 | 0.041 | 0.806 |
Number of reflections | 17716 | ||
<I/σ(I)> | 20.495 | ||
Completeness [%] | 99.9 | 99 | 100 |
Redundancy | 5.9 | 5.6 | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 25% PEG3350, 0.2M MgCl2, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |