3E1P

Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.

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	207.397, 207.397, 142.451
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	71.250 - 2.400
R-factor	0.241
Rwork	0.240
R-free	0.26000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2QP7 (APO-BFR)
RMSD bond length	0.012
RMSD bond angle	1.433
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]	73.320	2.530
High resolution limit [Å]	2.400	2.400
Number of reflections	117098
<I/σ(I)>	16.3	3.1
Completeness [%]	97.0	83.3
Redundancy	12	3.9

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. APO-BFR CRYSTALS WERE SUBSEQUENTLY (AEROBICALLY) SOAKED IN A CRYOPROTECTANT SOLUTION CONTAINING FE2+ (AND BUFFERED AT PH 7.0 WITH 0.1 M MOPS IN PLACE OF CITRATE) FOR 65 MINUTES BEFORE FALSH FREEZING AND DATA COLLECTION. PLEASE SEE PAPER FOR FULL DETAILS., PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, pH 5.00