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 |
