1K9B
Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 277 |
Detector technology | DIFFRACTOMETER |
Collection date | 1994-04-05 |
Detector | WEISSENBERG |
Wavelength(s) | 1.04 |
Spacegroup name | P 41 3 2 |
Unit cell lengths | 86.100, 86.100, 86.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.800 |
Rwork | 0.221 |
R-free | 0.30800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pi2 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.600 |
Data reduction software | ROTAVATA |
Data scaling software | WEIS |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.900 | 3.000 |
High resolution limit [Å] | 2.500 | 2.800 |
Rmerge | 0.058 | 0.300 |
Number of reflections | 26756 | |
Completeness [%] | 96.3 | 70 |
Redundancy | 6.88 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 289 | PEG 4000, ammonium sulfate, pH 7.6, VAPOR DIFFUSION, SITTING DROP at 289K |