7R66

Structure of Pfp1 protease from Thermococcus thioreducens: large unit cell at 1.44 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	173
Detector technology	PIXEL
Collection date	2019-06-15
Detector	DECTRIS EIGER X 500K
Wavelength(s)	1.1158
Spacegroup name	H 3
Unit cell lengths	151.030, 151.030, 80.716
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	68.690 - 1.440
R-factor	0.1355
Rwork	0.134
R-free	0.16590
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5txw
RMSD bond length	0.011
RMSD bond angle	1.174
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.19_4092)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	75.000	1.400
High resolution limit [Å]	1.380	1.380
Rmerge	0.216
Rmeas	0.221
Rpim	0.440
Number of reflections	141230	7080
<I/σ(I)>	11.9	0.3
Completeness [%]	100.0	100
Redundancy	47	19.8
CC(1/2)	0.999	0.073

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	298	Sitting drop crystallization using Cryschem plates. Drops were equal amounts of a 25 mg / ml protein stock solution in water and the reservoir solution. The reservoir was 1.4 M sodium citrate at pH 6.5. Crystallization was at room temperature. Drops were 10 ul total starting volume, reservoirs 0.6 ml.