1D2T
CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6B |
| Synchrotron site | Photon Factory |
| Beamline | BL-6B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-04-22 |
| Detector | FUJI |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 124.700, 124.700, 97.700 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 1.900 |
| R-factor | 0.215 |
| Rwork | 0.216 |
| R-free | 0.25700 |
| RMSD bond length | 0.017 * |
| RMSD bond angle | 0.017 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | MLPHARE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.074 * | 0.341 |
| Number of reflections | 34749 * | |
| <I/σ(I)> | 5.72 | |
| Completeness [%] | 92.7 | 74.4 |
| Redundancy | 4.2 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 20 * | drop contains protein and reservoir solution in a 1:1 ratio * |
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 | reservoir | PEG400 | 43-45 (%) | |
| 4 | 1 | reservoir | Tris-HCl | 0.1 (M) |
