3MBK
The 1.35 A Structure of the Phosphatase Domain of the Suppressor of T Cell Receptor Signalling Protein in Complex with Sulphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-09 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 62.966, 80.049, 105.448 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.940 - 1.350 |
| R-factor | 0.16323 |
| Rwork | 0.162 |
| R-free | 0.19062 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h0q |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.297 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.370 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.051 | 0.300 |
| Number of reflections | 115649 | |
| <I/σ(I)> | 32.4 | 3.3 |
| Completeness [%] | 98.3 | 83.5 |
| Redundancy | 5.8 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | 22 % PEG2000MME, 200 mM AmSO4 100 mM, NaAcetate pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
