1Z0E
Crystal Structure of A. fulgidus Lon proteolytic domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-07-20 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 48.680, 86.110, 135.610 |
Unit cell angles | 90.00, 94.70, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.050 |
R-factor | 0.21462 |
Rwork | 0.213 |
R-free | 0.29939 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.033 |
RMSD bond angle | 2.493 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.102 |
High resolution limit [Å] | 2.050 | 2.050 |
Number of reflections | 68204 | |
Completeness [%] | 96.5 | 76.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 295 | PEG 8000, calcium acetate, sodium cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |