6SV8
Terahertz irradiated structure of bovine trypsin (odd frames of crystal x38)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2) |
Synchrotron site | PETRA III, EMBL c/o DESY |
Beamline | P14 (MX2) |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-10-23 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.8856 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 53.440, 56.770, 65.430 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.920 - 1.150 |
Rwork | 0.130 |
R-free | 0.16800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 418G |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 42.920 | 42.920 | 1.180 |
High resolution limit [Å] | 1.150 | 5.160 | 1.150 |
Rmerge | 0.075 | 0.031 | 0.543 |
Rmeas | 0.083 | 0.035 | 0.699 |
Total number of observations | 636710 | ||
Number of reflections | 129886 | 1510 | 5398 |
<I/σ(I)> | 10.94 | 33.32 | 1.17 |
Completeness [%] | 96.1 | 99.7 | 53.8 |
Redundancy | 4.902 | 5.311 | 1.869 |
CC(1/2) | 0.999 | 0.999 | 0.524 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | protein solution- 60 mg/ml trypsin, 6 mg/ml benzamidine and 3 mM CaCl2 in a 30 mM HEPES buffer pH 7.0. Well solution- 18% PEG 8000, 200 mM (NH4)2SO4, 50 mM HEPES pH 7, 3 mM CaCl2 and 6 mg/ml benzamidine. 1:1 ratio drops |