1Z0W
Crystal Structure of A. fulgidus Lon proteolytic domain at 1.2A resolution
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 | 2004-11-05 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.99997 |
Spacegroup name | P 65 |
Unit cell lengths | 84.470, 84.470, 41.500 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 1.200 |
R-factor | 0.1372 |
Rwork | 0.137 |
R-free | 0.18090 |
Structure solution method | SAD |
RMSD bond length | 0.013 |
RMSD bond angle | 0.031 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.240 |
High resolution limit [Å] | 1.150 | 1.150 |
Rmerge | 0.070 | 0.683 |
Number of reflections | 52481 | |
<I/σ(I)> | 24.6 | 3.1 |
Completeness [%] | 95.6 | 94.4 |
Redundancy | 11.4 | 9.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 295 | PEG 8000,MES,calcium acetate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |