9GZU

Crystal structure of apo-bacterioferritin (Bfr) from Brucella melitentsis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 2
Synchrotron site	SOLEIL
Beamline	PROXIMA 2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-03-30
Detector	DECTRIS EIGER X 9M
Wavelength(s)	1.0439
Spacegroup name	F 4 3 2
Unit cell lengths	173.780, 173.780, 173.780
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.450 - 1.970
R-factor	0.1998
Rwork	0.198
R-free	0.23460
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	0.831
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.450	2.041
High resolution limit [Å]	1.970	1.970
Rmerge	0.149	1.363
Rmeas	0.150	1.372
Rpim	0.017	0.153
Number of reflections	16541	1585
<I/σ(I)>	36.62	4.67
Completeness [%]	100.0	99.94
Redundancy	76.7	79.1
CC(1/2)	1.000	0.946

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5	293	0.1M Hepes salt, 1.5M Lithium sulfate