1LRQ
Aquifex aeolicus KDO8P synthase H185G mutant in complex with PEP, A5P and Cadmium
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-01-23 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.5418 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 84.471, 84.471, 160.481 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 22.000 * - 1.800 |
Rwork | 0.207 |
R-free | 0.22800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 22.700 * |
Data scaling software | SCALEPACK |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.910 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.121 * | |
Total number of observations | 343217 * | |
Number of reflections | 59056 | |
<I/σ(I)> | 8.6 | |
Completeness [%] | 95.0 | 87.9 |
Redundancy | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 4. * | Duewel, H.S., (2001) J.Biol.Chem., 276, 8393. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 30 (mg/ml) | |
2 | 1 | reservoir | sodium acetate | 100 (mM) | |
3 | 1 | reservoir | PEG4000 | 5-6 (%) |