1TYF

THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	110
Detector technology	CCD
Collection date	1995-12
Spacegroup name	C 1 2 1
Unit cell lengths	193.320, 102.460, 157.080
Unit cell angles	90.00, 97.80, 90.00

Refinement procedure

Resolution	80.000 - 2.300
R-factor	0.219
Rwork	0.219
R-free	0.29200
RMSD bond length	0.008
RMSD bond angle	1.530
Data reduction software	HKL ((DENZO))
Data scaling software	HKL ((SCALEPACK))
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
Low resolution limit [Å]	80.000 *
High resolution limit [Å]	2.200 *
Rmerge	0.077
Number of reflections	142952 *
Completeness [%]	100.0
Redundancy	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.5 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10.4 (mg/ml)
2	1	drop	HEPES	10 (mM)
3	1	drop		200 (mM)
4	1	drop	dithiothreitol	1 (mM)
5	1	reservoir	Na citrate	100 (mM)
6	1	reservoir	PEG4000	10 (%(w/v))
7	1	reservoir	isopropanol	20 (%(v/v))