5IX6

X-ray structure of Auoxo3-encapsulated horse spleen apoferritin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	CCD
Collection date	2015-11-17
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	F 4 3 2
Unit cell lengths	180.645, 180.645, 180.645
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	104.300 - 1.850
R-factor	0.18256
Rwork	0.180
R-free	0.22596
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5erk
RMSD bond length	0.019
RMSD bond angle	1.752
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0049)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	104.300	1.880
High resolution limit [Å]	1.850	1.850
Rmerge	0.237
Rmeas	0.243
Rpim	0.102
Number of reflections	20893
<I/σ(I)>	9.2	0.8
Completeness [%]	99.5	95
Redundancy	6.9	3.4
CC(1/2)	0.666	0.284

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	293	Crystals of Auoxo3-encapsulated AFt with diamond-like morphology, suitable for X-ray diffraction data collection, were grown by hanging-drop vapor diffusion technique at 293 K mixing the protein (5-10 mg x mL-1) with equal volumes of a reservoir solution consisting of 0.6-0.8 M (NH4)2SO4, 0.1 M Tris pH 7.4-7.7, 50-60 mM CdSO4.