3T4U
L29I Mutation in an Aryl Esterase from Pseudomonas fluorescens Leads to Unique Peptide Flip and Increased Activity
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 4.2.2 |
| Synchrotron site | ALS |
| Beamline | 4.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-05-10 |
| Detector | NOIR-1 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 32 |
| Unit cell lengths | 145.883, 145.883, 128.587 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.230 - 2.020 |
| R-factor | 0.1939 |
| Rwork | 0.192 |
| R-free | 0.22130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1va4 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.390 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK (9.9.3L) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.090 |
| High resolution limit [Å] | 2.020 | 2.020 |
| Rmerge | 0.106 | 0.237 |
| Number of reflections | 200730 | |
| <I/σ(I)> | 5.7 | 2.9 |
| Completeness [%] | 98.7 | 97.6 |
| Redundancy | 3.01 | 2.77 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 1% PEG 400, 1.65M (NH4)2SO4, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
