3IO2
Crystal structure of the Taz2 domain of p300
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-12-04 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.2827 |
Spacegroup name | I 41 3 2 |
Unit cell lengths | 155.270, 155.270, 155.270 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.350 - 2.500 |
R-factor | 0.20802 |
Rwork | 0.206 |
R-free | 0.23639 |
Structure solution method | SAD |
RMSD bond length | 0.021 |
RMSD bond angle | 2.200 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.4.0077) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.093 | 0.647 |
Number of reflections | 11355 | |
<I/σ(I)> | 19.2 | 2.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 5.8 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 6.3 | 277 | Protein solution: 30 mg/ml Taz2, 25 mM MES pH 6.3, 100 mM NaCl, 6% glycerol, 10% TCEP. Precipitating solution: 3.2 M AMS in MES buffer pH 6.0, 10 % ethylene glycol. Both solutions mixed 1:1 and kept under oil, Microbatch, temperature 277K |