1Z0V
Crystal Structure of A. fulgidus Lon proteolytic domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-09-08 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.454, 86.279, 137.966 |
| Unit cell angles | 90.00, 92.30, 90.00 |
Refinement procedure
| Resolution | 15.000 - 3.000 |
| R-factor | 0.21947 |
| Rwork | 0.215 |
| R-free | 0.31016 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.041 |
| RMSD bond angle | 3.281 |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.075 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Number of reflections | 22682 | |
| Completeness [%] | 98.9 | 98.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | PEG 400,calcium acetate,sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
