2PK0
Structure of the S. agalactiae serine/threonine phosphatase at 2.65 resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-05-20 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.933 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 139.400, 92.100, 86.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.650 - 2.650 |
| R-factor | 0.2 |
| Rwork | 0.197 |
| R-free | 0.27121 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Manually built model from SAD phasing = S.a. STP with 70% of residues built |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.313 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.700 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmerge | 0.115 | 0.440 |
| Number of reflections | 32767 | |
| <I/σ(I)> | 11.7 | 3.7 |
| Completeness [%] | 99.5 | 99 |
| Redundancy | 5.2 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 0.2 M Mg acetate, 18% PEG 8000, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
