2I3R
Engineered catalytic domain of protein tyrosine phosphatase HPTPbeta
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-01-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.856, 71.643, 70.531 |
Unit cell angles | 90.00, 93.58, 90.00 |
Refinement procedure
Resolution | 31.900 - 1.850 |
R-factor | 0.184 |
Rwork | 0.184 |
R-free | 0.21700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2h02 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.390 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.900 | 1.950 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.032 | 0.162 |
Number of reflections | 51856 | |
<I/σ(I)> | 19.6 | 6.09 |
Completeness [%] | 98.5 | 99.9 |
Redundancy | 2.8 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 21% PEG 8000, 220 mM MgCl2, 1% BME, 0.1% BOG, 5mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 298K |