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 |