9PDA

Structure of Porcine Trypsin Crystals Grown From PEG and Complexed With Crystallization Additives IV

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	295
Detector technology	IMAGE PLATE
Collection date	2012-07-04
Detector	RIGAKU
Wavelength(s)	1.54
Spacegroup name	P 1 21 1
Unit cell lengths	70.660, 50.720, 125.690
Unit cell angles	90.00, 99.52, 90.00

Refinement procedure

Resolution	39.250 - 1.180
R-factor	0.1965
Rwork	0.195
R-free	0.23030
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.280
Data reduction software	d*TREK
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.21.1_5286)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.170	1.220
High resolution limit [Å]	1.180	1.180
Rmerge	0.061	0.346
Number of reflections	288012	800
<I/σ(I)>	14.3
Completeness [%]	91.1
Redundancy	4.81

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		295	Sitting drop vapor diffusion in Cryschem plates with reservoirs of 30% PEG 3350 buffered at pH 6.5 with 0.1 M HEPES. Drops composed of 3 ul reservoir, 2 ul of additive mix (oxalic acid, malic acid, oxaloacetic acid, pyromellitic acid), and 3 ul of a 40 mg/ml protein stock