5JNU
Crystal structure of mouse Low-Molecular Weight Protein Tyrosine Phosphatase type A (LMPTP-A) complexed with phosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-03 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9791 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.384, 77.152, 92.367 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.576 - 2.535 |
| R-factor | 0.2103 |
| Rwork | 0.208 |
| R-free | 0.25340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5jnr |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.562 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.7) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 38.580 | 38.580 | 2.650 |
| High resolution limit [Å] | 2.530 | 8.780 | 2.530 |
| Rmerge | 0.138 | 0.053 | 0.600 |
| Rmeas | 0.157 | ||
| Rpim | 0.074 | ||
| Total number of observations | 40453 | ||
| Number of reflections | 9354 | ||
| <I/σ(I)> | 6.7 | ||
| Completeness [%] | 99.5 | 98.8 | 96.4 |
| Redundancy | 4.3 | 3.8 | 3.3 |
| CC(1/2) | 0.985 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 5.5 | 293 | 7% PEG 10K, Bis Tris, Ammonium Acetate; soaked in NaPO4 buffer before data collection |
