8VCB

Crystal structure of a Bacteroides fragilis S41 protease

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-02-28
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9537
Spacegroup name	P 1 21 1
Unit cell lengths	63.397, 43.073, 119.743
Unit cell angles	90.00, 101.71, 90.00

Refinement procedure

Resolution	40.430 - 1.960
R-factor	0.1796
Rwork	0.177
R-free	0.22800
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.181
Data reduction software	XDS
Data scaling software	Aimless (0.7.8)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.730	2.010
High resolution limit [Å]	1.960	1.960
Rmerge	0.155	1.170
Rmeas	0.168	1.265
Rpim	0.063	0.475
Total number of observations	317968	21654
Number of reflections	46018	3124
<I/σ(I)>	9.4	1.7
Completeness [%]	99.9
Redundancy	6.9	6.9
CC(1/2)	0.997	0.735

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	289.15	0.15uL 9.1 mg/mL Q5LIA5 (10mM HEPES pH 7.5, 100mM NaCl) were mixed with 0.15 uL of reservoir solution. Sitting drop reservoir contained 25 uL of 0.1 M MES monohydrate pH 6.0 and 22% v/v Polyethylene glycol 400. Crystal was frozen in a solution of ~25% glycerol, 75% reservoir after ~10s soaking in that solution.