3E1L

Crystal structure of E. coli Bacterioferritin (BFR) soaked in phosphate with an alternative conformation of the unoccupied Ferroxidase centre (APO-BFR II).

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	208.082, 208.082, 143.107
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.000 - 2.500
R-factor	0.236
Rwork	0.236
R-free	0.24800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2QP7
RMSD bond length	0.012
RMSD bond angle	1.368
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]	34.200	2.640
High resolution limit [Å]	2.500	2.500
Number of reflections	104275
<I/σ(I)>	19.6	5.2
Completeness [%]	96.4	80.7
Redundancy	13.9	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	298	1.8 M AMMOMIUM SULFATE, 0.1 M TRI- SODIUM CITRATE PH 5.0. SUBSEQUENTLY, THE CRYSTALS WERE SOAKED IN A CRYO-PROTECTANT BUFFER CONTAINING PHOSPHATE BUFFERED WITH MOPS PH 7 INSTEAD OF CITRATE. SEE PAPER FOR FULL DETAILS., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, pH 5.00