2PRQ
X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-D |
Synchrotron site | APS |
Beamline | 14-BM-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-03-03 |
Detector | ADSC QUANTUM 1 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 106.200, 106.200, 96.700 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.150 |
R-factor | 0.224 |
Rwork | 0.224 |
R-free | 0.27300 |
Structure solution method | Model derived phases |
Starting model (for MR) | PDB code 1AMP |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.120 | 0.743 |
Number of reflections | 18085 | |
<I/σ(I)> | 6.5 | |
Completeness [%] | 99.9 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 100 mM Tris pH 8.0, 100 mM KSCN, 4.5 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298KK |