4OU3
Crystal structure of porcine aminopeptidase N complexed with CNGRCG tumor-homing peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 4.2.2 |
| Synchrotron site | ALS |
| Beamline | 4.2.2 |
| Detector technology | CCD |
| Collection date | 2013-01-14 |
| Detector | NOIR-1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 260.323, 62.879, 82.023 |
| Unit cell angles | 90.00, 100.59, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.950 |
| R-factor | 0.14285 |
| Rwork | 0.140 |
| R-free | 0.18956 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fke |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.614 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CCP4 |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.960 |
| High resolution limit [Å] | 1.920 | 1.920 |
| Rmerge | 0.079 | 0.615 |
| Number of reflections | 95642 | |
| <I/σ(I)> | 20.7 | 1.7 |
| Completeness [%] | 97.9 | 97 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 277 | 2 uL protein + 2 uL well solution (18% v/v PEG3350, 200 mM lithium sulfate, 100 mM HEPES, pH 7.2), VAPOR DIFFUSION, SITTING DROP, temperature 277K |
