2BV5
CRYSTAL STRUCTURE OF THE HUMAN PROTEIN TYROSINE PHOSPHATASE PTPN5 AT 1.8A RESOLUTION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-03-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 39.957, 64.010, 136.149 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 68.040 - 1.800 |
| R-factor | 0.166 |
| Rwork | 0.164 |
| R-free | 0.20100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bij |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.322 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.960 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.060 | 0.370 |
| Number of reflections | 32877 | |
| <I/σ(I)> | 12.9 | 2.5 |
| Completeness [%] | 98.7 | 95.4 |
| Redundancy | 4.9 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | SITTING DROP, 25% PEG3350, 0.2M LI2SO4, 100MM BIS TRIS PROPANE PH 5.5 |
