2HC1
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 |
Detector technology | CCD |
Collection date | 2005-01-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 39.060, 70.714, 118.455 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.880 - 1.300 |
R-factor | 0.136 |
Rwork | 0.134 |
R-free | 0.17885 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2h02 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.232 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.880 | 1.400 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.040 | 0.350 |
Number of reflections | 59896 | |
<I/σ(I)> | 15.32 | 2.85 |
Completeness [%] | 72.6 | 69.2 |
Redundancy | 1.2 | 0.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.2 | 298 | 20% PEG 8000, 220 mM MgCl2, 1% BME, 0.1% BOG, 5mM DTT, 180 mM Nh4OAc, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |