1EEN
CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH ACETYL-D-A-D-BPA-PTYR-L-I-P-Q-Q-G
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X9B |
| Synchrotron site | NSLS |
| Beamline | X9B |
| Temperature [K] | 140 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-05 |
| Detector | FUJI |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 66.348, 72.544, 88.466 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.780 - 1.900 |
| R-factor | 0.188 |
| Rwork | 0.188 |
| R-free | 0.21700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1aax |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.400 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.035 | 0.131 |
| Total number of observations | 160542 * | |
| Number of reflections | 32272 | 2160 * |
| <I/σ(I)> | 20.7 | 4.8 |
| Completeness [%] | 93.3 | 63.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 * | 4 * | pH 7.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | MES | 100 (mM) | |
| 3 | 1 | drop | 25 (mM) | ||
| 4 | 1 | drop | EDTA | 0.2 (mM) | |
| 5 | 1 | drop | dithiothreitol | 3.0 (mM) | |
| 6 | 1 | drop | peptide | 5 (mM) | |
| 7 | 1 | reservoir | HEPES | 0.1 (M) | |
| 8 | 1 | reservoir | magnesium acetate | 0.2 (M) | |
| 9 | 1 | reservoir | PEG8000 | 12-20 (%(w/v)) |
