2RC4
Crystal Structure of the HAT domain of the human MOZ protein
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-06-11 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9795, 1.2571, 1.2829, 1.2832 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 109.200, 109.200, 144.779 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 3.000 |
R-factor | 0.277 |
Rwork | 0.276 |
R-free | 0.28300 |
Structure solution method | MAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.505 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE (2.03) |
Refinement software | REFMAC (refmac_5.2.0005) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.770 |
High resolution limit [Å] | 2.670 | 5.750 | 2.670 |
Rmerge | 0.082 | 0.067 | 0.072 |
Number of reflections | 12178 | ||
<I/σ(I)> | 13.6 | ||
Completeness [%] | 95.2 | 94.7 | 62.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.5 | 298 | sodium cacodylate, PEG 3350, pH 6.5, VAPOR DIFFUSION, temperature 298K |
1 | VAPOR DIFFUSION | 6.5 | 298 | sodium cacodylate, PEG 3350, pH 6.5, VAPOR DIFFUSION, temperature 298K |