2IJZ
Crystal structure of aminopeptidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 200 |
Detector technology | CCD |
Collection date | 2006-09-23 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9795 |
Spacegroup name | P 1 |
Unit cell lengths | 134.678, 134.553, 134.601 |
Unit cell angles | 60.12, 60.10, 60.16 |
Refinement procedure
Resolution | 20.000 - 3.000 |
R-factor | 0.255 |
Rwork | 0.255 |
R-free | 0.29100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1u6l |
RMSD bond length | 0.007 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.900 |
High resolution limit [Å] | 2.700 | 2.730 |
Rmerge | 0.106 | 0.223 |
Number of reflections | 147805 | |
Completeness [%] | 87.0 | 83.6 |
Redundancy | 1.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 0.1M Sodium Citrate, 10% PEG 15K, pH 5.6, VAPOR DIFFUSION, HANGING DROP |