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 |