3R2T

2.2 Angstrom Resolution Crystal Structure of Superantigen-like Protein from Staphylococcus aureus subsp. aureus NCTC 8325.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2011-03-03
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 21 21 21
Unit cell lengths	51.701, 72.314, 123.960
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.630 - 2.210
R-factor	0.20753
Rwork	0.205
R-free	0.25210
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3kls
RMSD bond length	0.012
RMSD bond angle	1.569
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	BALBES
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.240
High resolution limit [Å]	2.200	2.200
Rmerge	0.076	0.501
Number of reflections	24026
<I/σ(I)>	19.6	3.8
Completeness [%]	99.9	100
Redundancy	6	6.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		295	Protein: 7.5mG/mL. 0.5M Sodium chloride, 0.01M Tris, pH 8.3. Screen: Classics II, G5, 0.2M Lithium Sulfate, 0.1M Tris, pH 8.5, 25% (w/v) PEG 3350 , VAPOR DIFFUSION, SITTING DROP, temperature 295K