2Q2F

Structure of the human Selenoprotein S (VCP-interacting membrane protein)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2007-04-15
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97927
Spacegroup name	C 1 2 1
Unit cell lengths	119.666, 18.705, 37.992
Unit cell angles	90.00, 93.36, 90.00

Refinement procedure

Resolution	31.200 - 1.500
R-factor	0.18291
Rwork	0.181
R-free	0.21434
Structure solution method	SAD
RMSD bond length	0.016
RMSD bond angle	1.498
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	SOLVE
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.200	1.550
High resolution limit [Å]	1.500	1.500
Number of reflections	13654
<I/σ(I)>	25.08	4.2
Completeness [%]	98.1	88
Redundancy	7	5.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	298	Protein buffer: 100mM NaCl, 50mM Tris-HCl pH 8.0, 1mM EDTA, 2mM CaCl2, 5mM Beta-mercaptoethanol. Crystallization buffer: 13% PEG2000 MME, 0.1M Sodium acetate pH 4.6, 0.1M KSCN. Cryo: 30% Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K