9F6H
Crystal structure of bovine alpha-chymotrypsin in complex with the bicyclic peptide inhibitor MP5.4.3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-11-29 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | P 61 |
| Unit cell lengths | 103.471, 103.471, 46.421 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.840 - 2.420 |
| R-factor | 0.21492 |
| Rwork | 0.212 |
| R-free | 0.28558 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.426 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.840 | 2.483 |
| High resolution limit [Å] | 2.420 | 2.420 |
| Rmerge | 0.137 | |
| Number of reflections | 10807 | 1132 |
| <I/σ(I)> | 10.5 | 1.6 |
| Completeness [%] | 98.0 | 98.6 |
| Redundancy | 6.1 | |
| CC(1/2) | 0.997 | 0.439 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 70% v/v MPD, 0.1 M HEPES, pH 7.5. |
