3BTH
THE CRYSTAL STRUCTURES OF THE COMPLEXES BETWEEN BOVINE BETA-TRYPSIN AND TEN P1 VARIANTS OF BPTI
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM1A |
| Synchrotron site | ESRF |
| Beamline | BM1A |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-04 |
| Detector | MARRESEARCH |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 75.540, 84.890, 122.660 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.750 |
| Rwork | 0.204 |
| R-free | 0.23500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ptc |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.810 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.8) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.840 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.062 | 0.319 |
| Number of reflections | 39824 | |
| <I/σ(I)> | 7.7 | 2.3 |
| Completeness [%] | 92.9 | 95.7 |
| Redundancy | 3.2 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | 37 * | pH 7.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 27 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 48-50 (%sat) | |
| 3 | 1 | reservoir | HEPES | 0.1 (M) |
