4PK1

Structure of BamB fused to a BamA POTRA domain fragment

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2012-08-06
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	49.270, 91.410, 61.210
Unit cell angles	90.00, 92.85, 90.00

Refinement procedure

Resolution	19.890 - 3.100
Rwork	0.251
R-free	0.28100
Structure solution method	MOLECULAR REPLACEMENT
Refinement software	PHENIX ((phenix.refine: 1.9_1692))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.900	3.150
High resolution limit [Å]	3.100	3.100
Number of reflections	9870
<I/σ(I)>	11	1.9
Completeness [%]	99.9	100
Redundancy	3.7	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		289	The BamA-BamB chimera protein was crystallized at 16 degC by sitting drop vapor diffusion method. Initial crystallizing conditions were refined in a hanging drop in the following solution: 1.4M Ammonium sulfate, 9% 2-propanol, and 0.1M Sodium acetate pH 5.5. We used 1.5 uL of the 20mg/ml protein mixed with 1.5 uL mother liquor in a reservoir filled with 500 uL precipitant solution