3OA1

Crystal structure of phosphoprotein/Protein P/Protein M1 residues 69-297 from Rabies virus reveals degradation to C-terminal domain only

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2010-07-29
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	91.980, 44.080, 74.580
Unit cell angles	90.00, 127.80, 90.00

Refinement procedure

Resolution	37.640 - 2.200
R-factor	0.1749
Rwork	0.172
R-free	0.22500
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.015
RMSD bond angle	1.382
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.260
High resolution limit [Å]	2.200	9.840	2.200
Rmerge	0.071	0.055	0.179
Number of reflections	11974	152	706
<I/σ(I)>	19.01	31.5	9.1
Completeness [%]	97.8	96.2	81.3
Redundancy	7		5.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	6.48 mg/mL LyraA.17086.a.D14 PD00142 in 25 mM Tris pH 8, 0.2 M NaCl, 1 mM TCEP, 1% glycerol against Emerald Biosystems Wizard Full screen condition A8 2 M ammonium sulphate, 0.1 M Citrate pH 5.5, 16 C, 0.4 uL protein and 0.4 uL precipitant, crystal tracking ID 216420a8, VAPOR DIFFUSION, SITTING DROP, temperature 289K