3IL0
The crystal structure of the aminopeptidase P,XAA-pro aminopeptidase from Streptococcus thermophilus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-17 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 43.303, 80.396, 100.858 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 62.870 - 2.200 |
| R-factor | 0.20314 |
| Rwork | 0.201 |
| R-free | 0.23688 |
| Structure solution method | SAD |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.929 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 62.870 | 2.257 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.133 | 0.640 |
| Number of reflections | 17521 | |
| <I/σ(I)> | 24.1 | 1.89 |
| Completeness [%] | 99.6 | 99.63 |
| Redundancy | 8.9 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 289 | 0.2M Calcium acetate hydrate, 20% w/v PEG 3350, 25% glycerol, temperature 289K |
