1Z0B
Crystal Structure of A. fulgidus Lon proteolytic domain E506A 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) | 1.000 |
Spacegroup name | P 65 |
Unit cell lengths | 83.260, 83.260, 41.170 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 1.550 |
R-factor | 0.18012 |
Rwork | 0.180 |
R-free | 0.20717 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.470 |
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 | 1.591 |
High resolution limit [Å] | 1.550 | 1.550 |
Number of reflections | 23792 | |
Completeness [%] | 99.9 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | PEG 400, calcium acetate, sodium cacodylate , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |