1QMT
Recombinant Human Eosinophil Cationic Protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.5 |
| Synchrotron site | SRS |
| Beamline | PX9.5 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-03-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 63 |
| Unit cell lengths | 100.159, 100.159, 31.281 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.400 |
| R-factor | 0.176 |
| Rwork | 0.176 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | EOSINOPHIL DERIVED NEUROTOXIN STRUCTURE AT 1.8 ANGSTROMS (COORDINATES NOT SUBMITTED) WAS PROVIDED BY S.MOSIMANN AND M.N.G.JAMES AND USED FOR MOLECULAR REPLACEMENT. |
| RMSD bond length | 0.010 |
| RMSD bond angle | 28.100 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.851) |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.107 | 0.287 |
| Total number of observations | 34137 * | |
| Number of reflections | 6916 | |
| <I/σ(I)> | 10.7 | 3.5 |
| Completeness [%] | 95.7 | 65 |
| Redundancy | 4.93 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | 16 * | microseeding * |
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) |
