4R8F
Crystal structure of yeast aminopeptidase 1 (Ape1)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL15A |
| Synchrotron site | NSRRC |
| Beamline | BL15A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-06-19 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 1.2 |
| Spacegroup name | H 3 |
| Unit cell lengths | 140.171, 140.171, 348.677 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 116.230 - 2.500 |
| R-factor | 0.2169 |
| Rwork | 0.215 |
| R-free | 0.24637 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4dyo |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.092 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 116.230 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.554 | |
| Number of reflections | 84889 | |
| <I/σ(I)> | 2.04 | |
| Completeness [%] | 96.6 | 98 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | 0.1M Tris-HCl pH7.2, 1.1M NaCl, 42.5% PEG 400, 0.1M MgCl2, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K |
