3E1N

Crystal structure of E. coli Bacterioferritin (BFR) after a 65 minute (aerobic) exposure to FE(II) revealing a possible MU-OXO bridge/MU-Hydroxy bridged DIIRON intermediate at the ferroxidase centre. (FE(III)-O-FE(III)-BFR).

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX10.1
Synchrotron site	SRS
Beamline	PX10.1
Temperature [K]	100
Detector technology	CCD
Collection date	2006-01-01
Spacegroup name	P 42 21 2
Unit cell lengths	207.741, 207.741, 142.951
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.670 - 2.800
R-factor	0.251
Rwork	0.250
R-free	0.26800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2QP7
RMSD bond length	0.017
RMSD bond angle	1.856
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.700	2.950
High resolution limit [Å]	2.800	2.800
Number of reflections	75629
<I/σ(I)>	13.6	5.2
Completeness [%]	98.1	91.9
Redundancy	11	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	298	1.8 M AMMONIUM SULFATE, 0.1 M TRI- SODIUM CITRATE PH 5.0. CRYSTALS OF OF APO-BFR WERE SUBSEQUENTLY SOAKED AEROBICALLY FOR 65 MINUTES IN A SOLUTION CONTAINING FE2+ AND BUFFERED WITH MOPS PH 7 INSTEAD OF CITRATE PH 5. AFTER 65MIN EXPOSURE TO IRON AND AIR, THE CRYSTAL WAS FLASH FROZEN IN LIQUID NITROGEN AND X-RAY DIFFRACTION DATA COLLECTED. SEE PAPER FOR FULL DETAILS., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, pH 5.00