3E1M

Crystal structure of E. coli Bacterioferritin (BFR) obtained after soaking APO-BFR crystals for 2.5 minutes in FE2+ (2.5M FE(II)-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	207.972, 207.972, 142.878
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.040 - 2.700
R-factor	0.242
Rwork	0.241
R-free	0.25900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.017
RMSD bond angle	1.760
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]	32.000	2.850
High resolution limit [Å]	2.700	2.700
Number of reflections	73181
<I/σ(I)>	14.4	4.7
Completeness [%]	85.3	46.8
Redundancy	7.4	4.3

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. SUBSEQUENTLY, APO-BFR CRYSTALS WERE SOAKED IN A CRYOPROTECTANCT CONTAINING FE2+ AND BUFFERED USING MOPS PH 7 IN PLACE OF CITRATE PH 5. EXPOSURE TO IRON WAS LIMITED TO 2.5 MINUTES BEFORE FLASH FREEZING IN LIQUID NITROGEN. SEE PAPER FOR FULL DETAILS., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, pH 5.00