6SVG

Terahertz irradiated structure of bovine trypsin (odd frames of crystal x41)

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	53.550, 56.990, 65.580
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.050 - 1.160
Rwork	0.141
R-free	0.18126
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]	43.050	43.050	1.180
High resolution limit [Å]	1.150	5.160	1.150
Rmerge	0.194	0.068	1.474
Rmeas	0.213	0.075	1.814
Total number of observations	730894
Number of reflections	129069	1524	4729
<I/σ(I)>	7.83	24.79	0.77
Completeness [%]	94.6	99.9	46.7
Redundancy	5.663	6.043	2.284
CC(1/2)	0.995	0.993	0.116

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