1NL3

CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM

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	2002-07-22
Detector	CUSTOM-MADE
Wavelength(s)	1.0332
Spacegroup name	P 62 2 2
Unit cell lengths	206.196, 206.196, 295.412
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.800
R-factor	0.19587
Rwork	0.193
R-free	0.25900 *
Structure solution method	MAD
RMSD bond length	0.010 *
RMSD bond angle	1.430 *
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	2.850
High resolution limit [Å]	2.750	2.750
Rmerge	0.096 *	0.461 *
Number of reflections	95337	8700 *
Completeness [%]	98.8	91.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	289	Tris.HCl, sodium formate, glycerol, 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 (%)