3CTZ
Structure of human cytosolic X-prolyl aminopeptidase
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-17A |
| Synchrotron site | Photon Factory |
| Beamline | BL-17A |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 71.444, 131.429, 169.076 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.620 - 1.600 |
| R-factor | 0.15599 |
| Rwork | 0.154 |
| R-free | 0.19568 |
| Structure solution method | MAD |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.276 |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.600 |
| Number of reflections | 104753 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 289 | 0.1M HEPES, 0.15M calcium chloride, 20% PEG 400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
