1L8K
T Cell Protein-Tyrosine Phosphatase Structure
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-04-10 |
Detector | MARRESEARCH |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 60.494, 60.494, 187.633 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.560 |
R-factor | 0.215 * |
Rwork | 0.215 |
R-free | 0.28800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 * |
RMSD bond angle | 2.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.600 |
High resolution limit [Å] | 2.560 | 2.560 |
Rmerge | 0.067 * | 0.381 * |
Number of reflections | 11665 | |
Completeness [%] | 97.5 | 82 |
Redundancy | 3.3 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | Peg 8000, Hepes, MgSO4, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris | 10 (mM) | pH7.5 |
3 | 1 | drop | 25 (mM) | ||
4 | 1 | drop | EDTA | 0.2 (mM) | |
5 | 1 | drop | dithiothreitol | 3 (mM) | |
6 | 1 | reservoir | HEPES | 0.05-0.25 (M) | pH8.0 |
7 | 1 | reservoir | magnesium acetate | 0.2 (M) | |
8 | 1 | reservoir | PEG8000 | 20 (%) | |
9 | 1 | reservoir | beta-mercaptoethanol | 0.1 (%) |