3V93
unliganded structure of TcrPDEC1 catalytic domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-01-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 130.342, 130.342, 388.853 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| Rwork | 0.216 |
| R-free | 0.22600 |
| Structure solution method | SAD |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.100 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELXS |
| Refinement software | CNS |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 30.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.101 |
| Number of reflections | 219103 |
| <I/σ(I)> | 8.4 |
| Completeness [%] | 94.4 |
| Redundancy | 8.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | The catalytic domain of the unliganded TcrPDEC1 (270-614) were crystallized by vapor diffusion against a well buffer of 20% PEG3350, 0.4 M Na formate, 0.2 M guanidine, 0.1 M MES pH 6.5 at 4oC. The hanging drops contain 2 L protein (10 mg/mL) and 2 L well buffer, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
