2NOV

Breakage-reunion domain of S.pneumoniae topo IV: crystal structure of a gram-positive quinolone target

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.91694
Spacegroup name	I 2 2 2
Unit cell lengths	136.920, 137.850, 326.020
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	500.000 - 2.670
Rwork	0.224
R-free	0.27580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ab4
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall
High resolution limit [Å]	2.670
Number of reflections	85197
Redundancy	5.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	298	The purified ParC55 protein was dialyzed against 20 mM Tris-HCl, pH 7.0, 200 mM NaCl, 10% glycerol, 1 mM beta-mercaptoethanol, 0.05% NaN3 then concentrated to 3-4 mg/ml. Hanging drops were formed by mixing equal volumes of protein and crystallization solutions (100 mM Tris-HCl, pH 5.5, 200 mM NaCl, 1 mM beta-mercaptoethanol, 0.05% NaN3 and 10% of 1:1 ethanol-isopropanol as precipitant). , VAPOR DIFFUSION, HANGING DROP, temperature 298.0K