4HS9
Methanol tolerant mutant of the Proteus mirabilis lipase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-06-06 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.099, 54.849, 96.013 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.630 - 1.800 |
| R-factor | 0.1726 |
| Rwork | 0.171 |
| R-free | 0.20520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.976 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.3.0) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 90.000 | 90.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 3.880 | 1.800 |
| Rmerge | 0.068 | 0.064 | 0.299 |
| Number of reflections | 23372 | ||
| <I/σ(I)> | 10.7 | ||
| Completeness [%] | 96.6 | 92.1 | 97 |
| Redundancy | 5.9 | 5.5 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 298 | 1X MMT Buffer pH 5.0, 20% PEG1500, vapor diffusion, hanging drop, temperature 298K |
