1YPH
High resolution structure of bovine alpha-chymotrypsin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-11-20 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.91 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.830, 77.510, 62.770 |
| Unit cell angles | 90.00, 106.30, 90.00 |
Refinement procedure
| Resolution | 28.600 - 1.340 |
| R-factor | 0.139 |
| Rwork | 0.139 |
| R-free | 0.18900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5CHA molecule B |
| RMSD bond length | 0.014 |
| RMSD bond angle | 0.034 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.600 | 1.410 |
| High resolution limit [Å] | 1.340 | 1.340 |
| Rmerge | 0.047 | 0.434 |
| Number of reflections | 87580 | |
| <I/σ(I)> | 19.6 | 2.1 |
| Completeness [%] | 97.1 | 95.9 |
| Redundancy | 2.9 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 298 | PEG 1500, Ammonium sulphate, citrate, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
