1KSF

Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ 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
Wavelength(s)	1.000
Spacegroup name	P 65
Unit cell lengths	124.107, 124.107, 97.042
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.600
R-factor	0.22075
Rwork	0.216
R-free	0.30400 *
RMSD bond length	0.016 *
RMSD bond angle	1.980 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.600	2.600
Rmerge		0.493
Number of reflections	22312
Completeness [%]	100.0	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	21 *	iso-propanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP at 294K
1	VAPOR DIFFUSION, HANGING DROP	7.5	21 *	iso-propanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP at 294K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	ammonium sulfate	50 (%sat)
10	1	reservoir	isopropanol	8 (%)
11	1	reservoir	sodium azide	0.01 (%)
2	1	drop	protein	12 (mg/ml)
3	1	drop	HEPES	0.1 (M)	pH7.5
4	1	drop	glycerol	10 (%)
5	1	drop	ATPgammaS	8 (mM)	or ADP
6	1	drop		40 (mM)
7	1	reservoir	HEPES	0.1 (M)	pH7.5
8	1	reservoir		0.5 (M)
9	1	reservoir	glycerol	5 (%)