6SVR
Reference structure of bovine trypsin (odd frames of crystal x28)
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 | 2015-10-22 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.8856 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 53.410, 56.860, 65.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.890 - 1.160 |
Rwork | 0.131 |
R-free | 0.17145 |
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] | 42.890 | 42.890 | 1.190 |
High resolution limit [Å] | 1.160 | 5.170 | 1.160 |
Rmerge | 0.083 | 0.039 | 0.724 |
Rmeas | 0.092 | 0.043 | 0.894 |
Total number of observations | 627113 | ||
Number of reflections | 127807 | 1498 | 4650 |
<I/σ(I)> | 10.55 | 33.15 | 1.16 |
Completeness [%] | 95.0 | 99.3 | 46.5 |
Redundancy | 4.907 | 5.287 | 2.248 |
CC(1/2) | 0.998 | 0.999 | 0.425 |
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 |