1IVN
E.coli Thioesterase I/Protease I/Lysophospholiase L1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 133 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9236 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 49.936, 49.936, 170.364 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.100 * - 1.900 |
Rwork | 0.229 |
R-free | 0.25200 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jrl |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 * |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.100 * | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.046 | 0.246 |
Number of reflections | 17893 * | |
<I/σ(I)> | 12.9 | 4.94 |
Completeness [%] | 97.0 | 87.2 |
Redundancy | 21.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7 * | 298 | 2-[N-morpholino]ethanesulfonic acid, PEGMME 5000, Ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 24.5 (mg/ml) | |
2 | 1 | 2 | sodium phosphate | 10 (mM) | pH7.0 |
3 | 1 | 2 | PEG5000 MME | 25.5 (%(w/w)) |