2GLJ
crystal structure of aminopeptidase I from Clostridium acetobutylicum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-01-01 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.978 |
Spacegroup name | P 1 |
Unit cell lengths | 121.708, 129.680, 222.728 |
Unit cell angles | 89.88, 90.00, 116.68 |
Refinement procedure
Resolution | 19.950 - 3.200 |
R-factor | 0.25 |
Rwork | 0.250 |
R-free | 0.29700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 2.800 |
Number of reflections | 311235 |
Completeness [%] | 78.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 7% EtOH, 0.05M NaCl, 0.01M MnCl2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |