3PGY
Serine hydroxymethyltransferase from Staphylococcus aureus, S95P mutant.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-10-10 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 69.081, 86.531, 301.806 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.700 - 1.920 |
| R-factor | 0.1677 |
| Rwork | 0.166 |
| R-free | 0.20760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2w7e |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.598 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.950 |
| High resolution limit [Å] | 1.920 | 5.210 | 1.920 |
| Rmerge | 0.085 | 0.032 | 0.807 |
| Number of reflections | 136110 | ||
| <I/σ(I)> | 8 | 2.02 | |
| Completeness [%] | 98.0 | 99.8 | 95.4 |
| Redundancy | 6.1 | 6.3 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.2 M tri-ammonium citrate, 20% PEG-3350, 10 mM glycine, 10 mM pyridoxal 5'-phosphate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
