3FO5

Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2008-06-26
Detector	ADSC QUANTUM 4
Wavelength(s)	0.933
Spacegroup name	C 2 2 21
Unit cell lengths	52.440, 130.080, 165.230
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.470 - 2.000
R-factor	0.20466
Rwork	0.202
R-free	0.25122
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	1.386
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.5.0044)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.100
High resolution limit [Å]	2.000	2.000
Rmerge	0.055	0.545
Number of reflections	37936
<I/σ(I)>	15.34	2.57
Redundancy	6.4	63.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	293	0.2M Magnesium chloride, 0.1M Bis-tris, pH5.5, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K
1	VAPOR DIFFUSION, SITTING DROP	5.5	293	0.2M Magnesium chloride, 0.1M Bis-tris, pH5.5, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K
2	VAPOR DIFFUSION, SITTING DROP	5.5	293	0.2M Ammonium formate, 20% PEG3350, pH5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K