6OSZ
High Resolution Structure of the Monoclinic Form of Thermomyces Lanuginosa Lipase Complexed with Its Catalytic Products
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 173 |
| Detector technology | PIXEL |
| Collection date | 2019-03-23 |
| Detector | DECTRIS PILATUS 300K |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 76.929, 89.937, 123.422 |
| Unit cell angles | 90.00, 94.49, 90.00 |
Refinement procedure
| Resolution | 76.690 - 1.430 |
| R-factor | 0.1504 |
| Rwork | 0.149 |
| R-free | 0.18520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tib |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.924 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19rc7_4070) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 77.000 | 1.450 |
| High resolution limit [Å] | 1.430 | 1.430 |
| Rmerge | 0.158 | 5.700 |
| Rmeas | 0.163 | 6.100 |
| Rpim | 0.036 | 1.660 |
| Number of reflections | 307462 | 15076 |
| <I/σ(I)> | 9.1 | 0.4 |
| Completeness [%] | 99.7 | 98.8 |
| Redundancy | 19.5 | 13.3 |
| CC(1/2) | 0.998 | 0.264 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | Sitting drop vapor diffusion at room temperature in 10 ul drops. Drops composed of equal amounts of stock protein solution, which was approximately 30 mg/ml lipase in the filtered culture media, and the reservoir solution. The latter was 20% PEG 3350 buffered at pH 6.5 with 0.10 M MES |
