3TC5
Selective targeting of disease-relevant protein binding domains by O-phosphorylated natural product derivatives
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 77 |
| Detector technology | PIXEL |
| Collection date | 2010-10-18 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 68.360, 68.360, 79.370 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.730 - 1.400 |
| R-factor | 0.17663 |
| Rwork | 0.175 |
| R-free | 0.21098 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2zr6 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.146 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.000 | 1.700 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.338 | |
| Number of reflections | 42028 | |
| <I/σ(I)> | 4.7 | |
| Completeness [%] | 98.3 | 96.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 2.2M Ammonium sulphate, 0.1M HEPES buffer, 1% PEG 400,pH 7.5, vapor diffusion, sitting drop, temperature 277K, VAPOR DIFFUSION, SITTING DROP |
