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 |
