1EI1

DIMERIZATION OF E. COLI DNA GYRASE B PROVIDES A STRUCTURAL MECHANISM FOR ACTIVATING THE ATPASE CATALYTIC CENTER

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	120
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	84.700, 137.400, 78.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 2.300
R-factor	0.171 *
Rwork	0.166
R-free	0.26600
RMSD bond length	0.008
RMSD bond angle	1.600
Data reduction software	XDS
Phasing software	AMoRE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.500
High resolution limit [Å]	2.300	2.300
Rmerge	0.044
Total number of observations	114762 *
Number of reflections	33856
<I/σ(I)>	26.4
Completeness [%]	80.0	56
Redundancy	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	4 *	PEG400, ammonium sulfate, ADPNP, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	HEPES	100 (mM)	pH7.5
2	1	reservoir	PEG400	4 (%)
3	1	reservoir	ammonium sulfate	0.2 (M)
4	1	drop	protein	20 (mg/ml)
5	1	drop	ADPNP	10 (mM)