1P2J
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 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9312 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 74.760, 81.360, 124.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.350 |
| R-factor | 0.164 |
| Rwork | 0.164 |
| R-free | 0.19400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3btg |
| RMSD bond length | 0.037 |
| RMSD bond angle | 2.390 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 14.980 | 1.420 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.055 | 0.209 |
| Number of reflections | 77696 | |
| <I/σ(I)> | 7.3 | 2.4 |
| Completeness [%] | 93.4 | 64.4 |
| Redundancy | 3.2 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 310 | 50% ammonium sulfate, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 310K |
