8SQP

Crystal Structure of Bacterioferritin (Bfr) from Brucella abortus (Apo, 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	P 4 3 2
Unit cell lengths	112.069, 112.069, 112.069
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	31.080 - 2.050
R-factor	0.1967
Rwork	0.196
R-free	0.21500
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.551
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]	45.750	2.110
High resolution limit [Å]	2.050	2.050
Rmerge	0.101	3.359
Rmeas	0.102	3.400
Rpim	0.016	0.523
Total number of observations	615703	49707
Number of reflections	15708	1190
<I/σ(I)>	28.2	1.5
Completeness [%]	100.0
Redundancy	39.2	41.8
CC(1/2)	1.000	0.661

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		291	Berkeley screen condition H3: 20% (w/v) PEG 3350, 100 mM Calcium chloride. BrabA.00028.a.A1.PW39164 at 10 mg/mL. Plate: 13090, well C3 drop 2. Puck: PSL-1806, Cryo: 30% PEG 3350 + crystallant