3A5J
Crystal structure of protein-tyrosine phosphatase 1B
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-5A |
Synchrotron site | Photon Factory |
Beamline | BL-5A |
Temperature [K] | 98 |
Detector technology | CCD |
Collection date | 2008-11-18 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.000 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 88.426, 88.426, 72.467 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 26.880 - 1.700 |
R-factor | 0.18995 |
Rwork | 0.188 |
R-free | 0.22857 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cma |
RMSD bond length | 0.025 |
RMSD bond angle | 2.180 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.051 | 0.252 |
Number of reflections | 36101 | |
<I/σ(I)> | 38.4 | 7.75 |
Completeness [%] | 98.9 | 93.6 |
Redundancy | 10.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | VAPOR DIFFUSION, HANGING DROP |