9X3C

Crystal structure of B. subtilis YdzF in reduced state

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	BRUKER AXS MICROSTAR
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2023-11-10
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.54179
Spacegroup name	C 2 2 21
Unit cell lengths	118.070, 119.030, 79.920
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.950 - 2.540
Rwork	0.243
R-free	0.30840
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.952
Data reduction software	iMOSFLM (7.4)
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0430)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	41.950	2.650
High resolution limit [Å]	2.540	2.540
Rmerge	0.082	0.404
Rmeas	0.100	0.488
Rpim	0.055	0.269
Number of reflections	18602	2217
<I/σ(I)>	7.3	2.5
Completeness [%]	98.6	97.8
Redundancy	3.04	3.07
CC(1/2)	0.989	0.575

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH		298	Protein buffer: 50 mM HEPES-Na, pH 7.5, 100 mM NaCl, 5% (v/v) glycerol, and 0.1 mM TCEP. Crystallization solution: 100 mM Sodium acetate trihydrate, pH 4.6, 2.0 M Sodium formate. Protein and crystallization solution were mixed in a 1:1 ratio (microbatch under 1:1 paraffin oil to silicon oil).