1P2Q
Structural consequences of accommodation of four non-cognate amino-acid residues in the S1 pocket of bovine trypsin and chymotrypsin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-06-19 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9312 |
| Spacegroup name | P 61 |
| Unit cell lengths | 99.570, 99.570, 205.220 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 25.000 - 1.800 |
| R-factor | 0.206 |
| Rwork | 0.206 |
| R-free | 0.22100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cbw |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.054 | 0.221 |
| Number of reflections | 103549 | |
| <I/σ(I)> | 7.7 | 2.9 |
| Completeness [%] | 97.9 | 97.8 |
| Redundancy | 2.4 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 298 | 50% ammonium sulfate, 0.1M Tris, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
