6SVN

Reference structure of bovine trypsin (even 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	0.130
R-free	0.17144
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	0.756
Rmeas	0.092	0.043	0.935
Number of reflections	127819	1498	4642
<I/σ(I)>	10.52	32.77	1.13
Completeness [%]	95.0	99.3	46.4
Redundancy	4.907	5.285	2.253
CC(1/2)	0.998	0.999	0.401

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