1WCH
Crystal structure of PTPL1 human tyrosine phosphatase mutated in colorectal cancer - evidence for a second phosphotyrosine substrate recognition pocket
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 101 |
Detector technology | CCD |
Collection date | 2003-11-23 |
Detector | MARRESEARCH |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 99.707, 59.193, 66.075 |
Unit cell angles | 90.00, 113.05, 90.00 |
Refinement procedure
Resolution | 19.900 - 1.850 |
R-factor | 0.177 |
Rwork | 0.177 |
R-free | 0.20400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1aax |
RMSD bond length | 0.009 |
RMSD bond angle | 1.600 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.050 | 0.263 |
Number of reflections | 29500 | |
<I/σ(I)> | 26.1 | 3.6 |
Completeness [%] | 97.6 | 82.8 |
Redundancy | 3.6 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION |