1PA1
Crystal structure of the C215D mutant of protein tyrosine phosphatase 1B
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-06-14 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.451, 88.451, 104.356 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 1.600 |
| R-factor | 0.19 |
| Rwork | 0.186 |
| R-free | 0.20400 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1pty |
| RMSD bond length | 0.010 |
| RMSD bond angle | 23.300 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CNX |
| Refinement software | CNX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.000 | 1.700 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.043 * | 0.269 * |
| Number of reflections | 62681 | 9061 * |
| <I/σ(I)> | 11.2 | 2.9 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 10. * | 9.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 4 * | PEG 3350, MgCl2, Hepes, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | HEPES | 20 (mM) | |
| 3 | 1 | drop | 50 | ||
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | drop | N,N'-dimethylbis(mercaptoacetyl)hydrazine | 5 (mM) | pH7.0 |
| 6 | 1 | reservoir | PEG3350 | 13-16 (%) | |
| 7 | 1 | reservoir | HEPES | 100 (mM) | |
| 8 | 1 | reservoir | 200 (mM) | pH7.0 |
