3O5V
The Crystal Structure of the Creatinase/Prolidase N-terminal domain of an X-PRO dipeptidase from Streptococcus pyogenes to 1.85A
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 | 2010-01-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 79.439, 79.439, 88.823 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 36.260 - 1.850 |
| R-factor | 0.194 |
| Rwork | 0.192 |
| R-free | 0.22400 |
| Structure solution method | SAD |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.220 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 3.990 | 1.850 |
| Rmerge | 0.057 | 0.036 | 0.593 |
| Number of reflections | 27878 | ||
| <I/σ(I)> | 12.7 | ||
| Completeness [%] | 99.5 | 95.7 | 100 |
| Redundancy | 4.8 | 4.4 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 297 | 17% PEG 10,0000, 0.1M Bis-Tris pH 5.5, 0.1M Ammonium acetate, VAPOR DIFFUSION, SITTING DROP, temperature 297K |
