4AV7
Structure determination of the double mutant S233Y F250G from the sec- alkyl sulfatase PisA1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-12 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.201, 201.955, 248.495 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.650 - 3.000 |
| R-factor | 0.19 |
| Rwork | 0.186 |
| R-free | 0.25591 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2yhe |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.316 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.760 | 3.110 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmerge | 0.070 | 0.540 |
| Number of reflections | 79645 | |
| <I/σ(I)> | 10.8 | 2 |
| Completeness [%] | 78.4 | 79.4 |
| Redundancy | 3 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.5 | 10 MG/ML PROTEIN, 0.1 M SODIUM ACETATE PH 4.7, 30% W/V PEG 2000 |
