4GXH
Crystal Structure of a Pyrrolidone-carboxylate peptidase 1 (target ID NYSGRC-012831) from Xenorhabdus bovienii SS-2004
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2012-04-27 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.075 |
| Spacegroup name | P 43 2 2 |
| Unit cell lengths | 117.179, 117.179, 186.615 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.691 - 2.700 |
| R-factor | 0.1782 |
| Rwork | 0.176 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | A low resolution de-novo phased structure |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.383 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.750 |
| High resolution limit [Å] | 2.700 | 7.320 | 2.700 |
| Rmerge | 0.091 | 0.037 | 0.890 |
| Number of reflections | 40725 | ||
| <I/σ(I)> | 14.5 | ||
| Completeness [%] | 99.9 | 99.1 | 100 |
| Redundancy | 5.3 | 5.4 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 293 | 0.2 M Na2HPO4/KH2PO4, 2.5 M Sodium Chloride, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
