9BKF
Crystal structure of selenomethionine labeled bovine trypsin mutant - S195A solved by Sulphur-SAD at 1A wavelength
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-02-26 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 54.708, 54.708, 107.174 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 21.720 - 1.200 |
R-factor | 0.185 |
Rwork | 0.184 |
R-free | 0.20140 |
Structure solution method | SAD |
RMSD bond length | 0.004 |
RMSD bond angle | 0.784 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AutoSol |
Refinement software | PHENIX (1.21_5207) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.240 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.097 | 0.559 |
Number of reflections | 58229 | 5402 |
<I/σ(I)> | 28.94 | 3.39 |
Completeness [%] | 98.8 | |
Redundancy | 19.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | 0.1M Imidazole, pH 7.0 , 0.3M Ammonium Sulfate, 30% PEG8000 |