3BTW
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 | 75.670, 84.780, 122.990 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.050 |
| Rwork | 0.191 |
| R-free | 0.23800 |
| 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 | 2.160 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.082 | 0.306 |
| Number of reflections | 24572 | |
| <I/σ(I)> | 6.5 | 2.4 |
| Completeness [%] | 96.5 | 98 |
| Redundancy | 2.8 | 2.7 |
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) |
