4PV4
Proline aminopeptidase P II from Yersinia pestis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-02-26 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 124.299, 82.865, 110.091 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.400 - 1.760 |
| R-factor | 0.1615 |
| Rwork | 0.160 |
| R-free | 0.19770 |
| Structure solution method | SAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.686 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.400 | 50.000 | 1.810 |
| High resolution limit [Å] | 1.760 | 4.830 | 1.780 |
| Rmerge | 0.092 | 0.050 | 0.816 |
| Number of reflections | 110591 | ||
| <I/σ(I)> | 11.7 | 1.98 | |
| Completeness [%] | 99.7 | 98.5 | 99.8 |
| Redundancy | 5.4 | 5.3 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | 0.1 M Bis-Tris-HCl buffer, 25% PEG 3350, 5 mM proline, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
