2CE3

CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	77
Detector technology	CCD
Collection date	2005-07-10
Detector	ADSC CCD
Spacegroup name	P 1 21 1
Unit cell lengths	97.719, 168.948, 104.364
Unit cell angles	90.00, 114.83, 90.00

Refinement procedure

Resolution	169.030 - 2.600
R-factor	0.205
Rwork	0.202
R-free	0.26100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2cby
RMSD bond length	0.012
RMSD bond angle	1.387
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.500	2.690
High resolution limit [Å]	2.600	2.600
Rmerge	0.080	0.450
Number of reflections	90593
<I/σ(I)>	10	1.7
Completeness [%]	100.0	86
Redundancy	6	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5		THE PROTEIN WAS CRYSTALLIZED BY THE SITTING DROP METHOD WITH 400NL PROTEIN PLUS 400NL MOTHERLIQUOR AND 100UL RESERVOIR. CONDITION WAS IDENTIFIED USING A SET OF RANDOM CONDITIONS GENERATED WITH CRYSTOOL SOFTWARE AND OPTIMIZED TO 9.576% (W/V) PEG 2000 0.2M LITHIUM SULFATE 0.1M MOPS (4-MORPHOLINEPROPANESULFONIC ACID) PH 6.5 WITH CRYSTOOL BY REDUCING THE PARAMETER SPACE TO THE REAGENTS UTILIZED. CRYSTALS SHOWED AFTER 2 DAYS