2HPO
Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-11-14 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9797, 0.9798, 0.9612 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 120.438, 120.438, 170.561 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.940 - 1.650 |
R-factor | 0.15781 |
Rwork | 0.157 |
R-free | 0.18062 |
Structure solution method | MAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.171 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SHELXS |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.680 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.520 | 0.500 |
Number of reflections | 164250 | |
<I/σ(I)> | 14.1 | 2 |
Completeness [%] | 95.5 | 89.2 |
Redundancy | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 1.8 M Sodium Malonate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |