1NKT

CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEX WITH ADPBS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	173
Detector technology	CCD
Collection date	2002-07-21
Detector	CUSTOM-MADE
Wavelength(s)	1.0332
Spacegroup name	P 62 2 2
Unit cell lengths	206.050, 206.050, 292.857
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	99.000 * - 2.600 *
R-factor	0.21574
Rwork	0.213
R-free	0.26500 *
Structure solution method	MAD
RMSD bond length	0.020 *
RMSD bond angle	1.560 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.1.25)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000 *	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.089 *	0.480 *
Total number of observations	139810 *
Number of reflections	13803 *	13803 *
Completeness [%]	98.1	98.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	289	Tris.HCl, sodium formate, glycerol, magnesium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 289.0K
1	VAPOR DIFFUSION, HANGING DROP	7.5	289	Tris.HCl, sodium formate, glycerol, magnesium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 289.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	Tris-HCl	10 (mM)	pH7.5
2	1	reservoir	sodium formate	3.5-3.7 (M)
3	1	reservoir	glycerol	5-10 (%)