6F2F

Crystal structure of Protease 1 from Pyrococcus Horikoshii co-cystallized in presence of 10 mM Tb-Xo4 and ammonium sulfate.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2015-11-24
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97974
Spacegroup name	P 41 21 2
Unit cell lengths	124.588, 124.588, 128.866
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.770 - 1.650
R-factor	0.161
Rwork	0.161
R-free	0.17000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1g2i
RMSD bond length	0.010
RMSD bond angle	1.050
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	BUSTER (2.10.3)

Data quality characteristics

	Overall
Low resolution limit [Å]	44.770
High resolution limit [Å]	1.650
Rpim	0.031
Number of reflections	121190
<I/σ(I)>	14.4
Completeness [%]	99.8
Redundancy	11.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	1.9 to 2.4 ammonium sulfate, 0.2 M sodium potassium tartrate, 100 mM trisodium citrate dehydrate pH 5.6. 10 mM Tb-Xo4 were solubilized with the protein solution prior to perform crystallization drops.