8IIY
Crystal structure of MBP fused GAS41 YEATS domain in complex with H3K14ac peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-08-02 |
Detector | RAYONIX MX225-HS |
Wavelength(s) | 1.000 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 66.241, 66.241, 248.821 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.000 - 2.150 |
R-factor | 0.17359 |
Rwork | 0.170 |
R-free | 0.24671 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 1.174 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.220 |
High resolution limit [Å] | 2.150 | 2.150 |
Number of reflections | 35680 | 3067 |
<I/σ(I)> | 14.5 | |
Completeness [%] | 100.0 | |
Redundancy | 11 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 100 mM Tris buffer (pH 8.5) containing 20% (w/v) PEG monomethyl ether 2000, 200 mM trimethylamine N-oxide |