3Q6D
Xaa-Pro dipeptidase from Bacillus anthracis.
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 | 2010-07-12 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 59.502, 107.912, 252.850 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.900 - 1.970 |
| R-factor | 0.19816 |
| Rwork | 0.196 |
| R-free | 0.24660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wy2 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.618 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 45.900 | 50.000 | 1.990 |
| High resolution limit [Å] | 1.960 | 5.320 | 1.960 |
| Rmerge | 0.082 | 0.039 | 0.501 |
| Number of reflections | 113973 | ||
| <I/σ(I)> | 10.9 | 2.24 | |
| Completeness [%] | 97.8 | 98.1 | 89.5 |
| Redundancy | 5.1 | 5.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 289 | 0.2 M calcium acetate, 0.1 M MES buffer, 20% PEG 8000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
