3PUU
Crystal Structure of Glu121Gln mutant of E. coli Aminopeptidase N
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-05-05 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 120.764, 120.764, 170.844 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 49.330 - 2.150 |
R-factor | 0.15372 |
Rwork | 0.152 |
R-free | 0.18717 |
Starting model (for MR) | 2hpo |
RMSD bond length | 0.016 |
RMSD bond angle | 1.427 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | REFMAC (5.2.0019) |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.082 | |
Number of reflections | 151714 | |
<I/σ(I)> | 25.5 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.8 | 298 | 1.0M ammonium sulfate, 50mM Hepes, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |