2YYS
Crystal structure of the proline iminopeptidase-related protein TTHA1809 from Thermus thermophilus HB8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-04-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 126.930, 126.930, 114.295 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.17812 |
| Rwork | 0.177 |
| R-free | 0.20835 |
| Structure solution method | SAD |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.229 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 2.200 |
| Number of reflections | 51211 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | 100mM HEPES-Na, 0.85M potassium sodium tartrate tetrahydrate, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
