1V2G
The L109P mutant of E. coli Thioesterase I/Protease I/Lysophospholipase L1 (TAP) in complexed with octanoic acid
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 |
| Collection date | 2000-05-30 |
| Detector | MAC Science DIP-2030 |
| Wavelength(s) | 1.12720 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 49.978, 49.978, 171.491 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.810 - 2.000 |
| Rwork | 0.225 |
| R-free | 0.26500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jrl |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.100 |
| Data reduction software | XPRESS |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.810 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.056 | 0.458 |
| Number of reflections | 14724 | |
| <I/σ(I)> | 12.1 | 3.2 |
| Completeness [%] | 97.1 | 97.8 |
| Redundancy | 9.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 2-[N-morpholino]ethanesulfonic acid, PEGMME5K, Ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
