2R7J

Crystal Structure of rotavirus non structural protein NSP2 with H225A mutation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9793990
Spacegroup name	I 4 2 2
Unit cell lengths	106.963, 106.963, 151.147
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.600
Rwork	0.226
R-free	0.27850
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1l9v
RMSD bond length	0.007
RMSD bond angle	1.198
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.700
High resolution limit [Å]	2.600	2.600
Rmerge	0.062	0.400
Number of reflections	13859
<I/σ(I)>	15.2	2.9
Redundancy	8.01	7.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.3	298	Protein:precipitant ratio 1:1 ;precipitant: 15% PEG 6000, 0.2M Magnesium acetate, 0.1M Tris-HCl; Protein buffer 0.2M MgCl2, 0.5mM EDTA, 0.5mM DTT, 2mM Tris-HCl, pH7.3, VAPOR DIFFUSION, HANGING DROP, temperature 298K