1H1H
Crystal Structure of Eosinophil Cationic Protein in Complex with 2',5'-ADP at 2.0 A resolution Reveals the Details of the Ribonucleolytic Active site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2000-08-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 63 |
| Unit cell lengths | 100.700, 100.700, 31.700 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.000 * - 2.000 |
| R-factor | 0.205 |
| Rwork | 0.205 |
| R-free | 0.21000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qmt |
| RMSD bond length | 0.006 |
| RMSD bond angle | 23.900 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.078 | 0.370 |
| Total number of observations | 61821 * | |
| Number of reflections | 12663 | |
| <I/σ(I)> | 14.7 | 2.92 |
| Completeness [%] | 99.4 | 99.9 |
| Redundancy | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | 16 * | microseeding, Boix, E., (1999) Biochemistry, 38, 16794. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 13 (mg/ml) | |
| 2 | 1 | reservoir | 0.5 (M) | ||
| 3 | 1 | reservoir | 2-propanol | 10 (%) | |
| 4 | 1 | reservoir | HEPES | 0.1 (M) |
