1J00
E. coli Thioesterase I/Protease I/Lysophospholipase L1 in complexed with diethyl phosphono moiety
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL17B2 |
Synchrotron site | NSRRC |
Beamline | BL17B2 |
Temperature [K] | 133 |
Detector technology | IMAGE PLATE |
Detector | MAC Science DIP-2030 |
Wavelength(s) | 1.12714 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 49.907, 49.907, 171.898 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 * - 2.000 |
Rwork | 0.239 |
R-free | 0.26700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jrl |
RMSD bond length | 0.007 * |
RMSD bond angle | 1.200 * |
Data reduction software | XPRESS |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 * | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.060 * | 0.381 |
Number of reflections | 15230 * | |
<I/σ(I)> | 11.3 | 5.2 |
Completeness [%] | 97.7 * | 98.9 |
Redundancy | 13.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7 * | 298 | 2-[N-morpholino]ethanesulfonic acid, PEGMME5000, 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)) |