1K6K

Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X9B
Synchrotron site	NSLS
Beamline	X9B
Temperature [K]	100
Detector technology	CCD
Detector	ADSC QUANTUM 4
Spacegroup name	P 21 21 21
Unit cell lengths	36.021, 51.965, 65.100
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 * - 1.800
Rwork	0.214
R-free	0.26300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	ClpA N-domain
RMSD bond length	0.005
RMSD bond angle	1.010 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	14.000
High resolution limit [Å]	1.800
Rmerge	0.028 *	0.199 *
Number of reflections	7990 *
Completeness [%]	67.2 *	21.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	21.5-22.5 *	VAPOR DIFFUSION, HANGING DROP, pH 7.0 at 294K
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	21.5-22.5 *	VAPOR DIFFUSION, HANGING DROP, pH 7.0 at 294K
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	21.5-22.5 *	VAPOR DIFFUSION, HANGING DROP, pH 7.0 at 294K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	ammonium sulfate	60 (%)
2	1	drop	HEPES	20 (mM)	pH7.5
3	1	reservoir	PIPES	0.1 (M)	pH7.0
4	1	reservoir	PEG8000	35 (%)
5	1	reservoir	sodium citrate	0.32 (M)