4P15

Structure of the ClpC N-terminal domain from an alkaliphilic Bacillus lehensis G1 species

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2012-12-06
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.54178
Spacegroup name	P 65
Unit cell lengths	84.620, 84.620, 32.150
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	36.641 - 1.850
R-factor	0.2114
Rwork	0.210
R-free	0.24040
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.955
Refinement software	PHENIX ((phenix.refine: 1.8.2_1309))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	73.290	73.290
High resolution limit [Å]	1.850	1.850
Rmerge	0.058	0.058
Number of reflections	11473
<I/σ(I)>	19.6	19.6
Completeness [%]	99.6	99.6
Redundancy	6.85	6.85

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.2	292.15	Protein crystallization was carried out using the hanging-drop vapor-diffusion method using 24-well Limbro tissue culture plates (ICN Inc.) at 19C. Drops were formed by mixing equal volumes (1 ul) of protein solution at 50 mg/mL and the reservoir solution containing 0.1M phosphate-citrate pH 4.2 20% polyethylene glycol 1000, 0.2M lithium sulphate. Hexagonal crystals appeared after 20-30 days