4ZBJ
UBN1 peptide bound to H3.3/H4/Asf1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-01-18 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 90.024, 90.024, 120.734 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.406 - 2.248 |
R-factor | 0.2095 |
Rwork | 0.208 |
R-free | 0.23480 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2hue |
RMSD bond length | 0.003 |
RMSD bond angle | 0.637 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX (1.8.4_1496) |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.406 | 2.330 |
High resolution limit [Å] | 2.248 | 2.250 |
Rmerge | 0.054 | 0.440 |
Number of reflections | 26431 | |
<I/σ(I)> | 26.4 | 2.7 |
Completeness [%] | 99.1 | 93.3 |
Redundancy | 6 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 295 | 0.1 M Sodium Cacodylate pH 6.0, 8% PEG 8K, 0.2 M NaCl |