5MC2
Crystal Structure of Gly278Asp mutant of Human Prolidase with Mn ions and GlyPro ligand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-01-09 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 103.842, 108.247, 211.187 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.170 - 1.700 |
| R-factor | 0.141 |
| Rwork | 0.141 |
| R-free | 0.17100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5m4j |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.992 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.165 | 1.800 |
| High resolution limit [Å] | 1.698 | 1.700 |
| Rmerge | 0.070 | 1.083 |
| Number of reflections | 130410 | |
| <I/σ(I)> | 19.88 | 1.85 |
| Completeness [%] | 99.8 | 98.9 |
| Redundancy | 7.51 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.4 | 278 | 10mM NaBorate, 760mM NaCitrate |
