8B61

Crystal structure of BfrC protein from Bacteroides fragilis NCTC 9343

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I24
Synchrotron site	Diamond
Beamline	I24
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-09-26
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.99
Spacegroup name	P 2 21 21
Unit cell lengths	52.075, 89.840, 99.056
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	66.550 - 1.810
R-factor	0.20378
Rwork	0.201
R-free	0.25069
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	alpha fold
RMSD bond length	0.013
RMSD bond angle	1.697
Data reduction software	xia2
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	66.550	1.840
High resolution limit [Å]	1.810	1.810
Rmerge	0.150	1.421
Rmeas	0.178	1.800
Rpim	0.071	0.871
Number of reflections	43116	2286
<I/σ(I)>	6.1	0.7
Completeness [%]	99.4	91.6
Redundancy	6	3.9
CC(1/2)	0.996	0.372

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	0.02 M M Magnesium chloride hexahydrate, 0.1M HEPES at pH 7.5 and 22 % w/v Poly acrylic acid sodium salt 5100