1Z0C
Crystal Structure of A. fulgidus Lon proteolytic domain D508A mutant
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 | 2005-02-16 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 65 |
| Unit cell lengths | 81.960, 81.960, 41.500 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 1.550 |
| R-factor | 0.21163 |
| Rwork | 0.209 |
| R-free | 0.25623 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.760 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.590 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Number of reflections | 23366 | |
| Completeness [%] | 100.0 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | PEG 600, calcium acetate, sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
