2ANE
Crystal structure of N-terminal domain of E.Coli Lon Protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-08-04 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 90.610, 53.445, 111.973 |
Unit cell angles | 90.00, 107.50, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.030 |
Rwork | 0.212 |
R-free | 0.26800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.860 |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.100 |
High resolution limit [Å] | 2.030 | 2.030 |
Rmerge | 0.352 | |
Number of reflections | 63721 | |
<I/σ(I)> | 38 | 3.1 |
Completeness [%] | 95.8 | 78.3 |
Redundancy | 4.7 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9.5 | 298 | PEG8000, CHES, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |