8SQT

Crystal Structure of Bacterioferritin (Bfr) from Brucella abortus (iron bound, cubic form 2, F16L mutant)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-03-14
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9795
Spacegroup name	F 4 3 2
Unit cell lengths	170.718, 170.718, 170.718
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.280 - 2.200
R-factor	0.1972
Rwork	0.194
R-free	0.26220
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.070
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.21rc1_4933: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.280	2.270
High resolution limit [Å]	2.200	2.200
Rmerge	0.142	2.706
Rmeas	0.143	2.740
Rpim	0.023	0.423
Total number of observations	441158	39929
Number of reflections	11356	962
<I/σ(I)>	26.3	1.9
Completeness [%]	100.0
Redundancy	38.8	41.5
CC(1/2)	1.000	0.693

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.5	291	Berkeley G7: 1.5M ammonium sulfate, 5% (v/v) MPD, 100 mM sodium acetate pH 4.5, BrabA.00028.a.A1.PW39164 at 10 mg/mL. Plate: 10390, well G7 drop 2. Puck: PSL-1812, Cryo: 2.5M lithium sulfate. 10 minute soak in 25 mM ferrous ammonium sulfate in cryo