3BTG
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 | 75.470, 84.660, 122.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.900 |
Rwork | 0.199 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ptc |
RMSD bond length | 0.010 |
RMSD bond angle | 1.890 |
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 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.069 | 0.327 |
Number of reflections | 31215 | |
<I/σ(I)> | 7.6 | 2.1 |
Completeness [%] | 99.3 | 99.6 |
Redundancy | 3 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 0.1 M HEPES PH 7.5 48% AMMONIUM SULPHATE |