2Y6T
Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-01-20 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 97.310, 48.278, 174.636 |
| Unit cell angles | 90.00, 103.96, 90.00 |
Refinement procedure
| Resolution | 169.480 - 2.740 |
| R-factor | 0.24741 |
| Rwork | 0.244 |
| R-free | 0.31444 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 4CHA AND 1ECZ |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.952 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 169.480 | 2.840 |
| High resolution limit [Å] | 2.740 | 2.740 |
| Rmerge | 0.080 | 0.210 |
| Number of reflections | 42247 | |
| <I/σ(I)> | 13.27 | 5.51 |
| Completeness [%] | 97.5 | 96.9 |
| Redundancy | 3.2 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | RESERVOIR SOLUTION - 100 MM BIS TRIS PH 5.5, 200 MM AMMONIUM SULPHATE, 17.5% PEG3350. PROTEIN SOLUTION - 3 MG/ML ECOTIN, 6 MG/ML CHYMOTRYPSIN IN 5MM TRIS PH 7.5. DROP - 1:1 VOLUME RATIO RESERVOIR:PROTEIN. |
