1EW2
CRYSTAL STRUCTURE OF A HUMAN PHOSPHATASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LURE BEAMLINE D41A |
Synchrotron site | LURE |
Beamline | D41A |
Temperature [K] | 80 |
Detector technology | IMAGE PLATE |
Collection date | 1997-04-24 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 88.800, 114.500, 106.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 22.000 - 1.820 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.24200 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 22.000 | 1.740 |
High resolution limit [Å] | 1.820 * | 1.820 * |
Rmerge | 0.082 * | 0.488 * |
Number of reflections | 41585 * | |
<I/σ(I)> | 8.5 | |
Completeness [%] | 79.6 | 67.6 * |
Redundancy | 2.34 | 1.32 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6 | 293 | PEG, pH 6.0, VAPOR DIFFUSION, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10-16 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 10 (mM) | |
3 | 1 | drop | 2 (mM) | ||
4 | 1 | drop | 0.02 (%) | ||
5 | 1 | reservoir | PEG4000 | 12 (%) | |
6 | 1 | reservoir | zinc acetate | 2 (mM) | |
7 | 1 | reservoir | imidazole malate | 200 (mM) |