1P2I
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 BM1A |
| Synchrotron site | ESRF |
| Beamline | BM1A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-04-04 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 74.700, 81.000, 124.090 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.410 - 1.650 |
| R-factor | 0.201 |
| Rwork | 0.201 |
| R-free | 0.21000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3btg |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.330 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.410 | 1.740 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.062 | 0.316 |
| Number of reflections | 45488 | |
| <I/σ(I)> | 9.7 | 2.4 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 4.3 | 4.3 |
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 |
