3I36
Crystal Structure of Rat Protein Tyrosine Phosphatase eta Catalytic Domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LNLS BEAMLINE D03B-MX1 |
Synchrotron site | LNLS |
Beamline | D03B-MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-01-01 |
Detector | MAR CCD 165 mm |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.468, 63.113, 111.655 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.715 - 1.841 |
R-factor | 0.1592 |
Rwork | 0.157 |
R-free | 0.20230 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ahs |
RMSD bond length | 0.009 |
RMSD bond angle | 1.237 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 37.420 | 1.940 |
High resolution limit [Å] | 1.840 | 1.840 |
Rmerge | 0.058 | 0.238 |
Number of reflections | 28395 | |
<I/σ(I)> | 9.1 | 4.5 |
Completeness [%] | 97.6 | 95 |
Redundancy | 3.5 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 291 | 20% PEG 10000, 0.1M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |