5E2X

The crystal structure of the C-terminal domain of Ebola (Tai Forest) nucleoprotein

Replaces:  5CII

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
Collection date	2014-11-06
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.979
Spacegroup name	P 1
Unit cell lengths	57.847, 60.075, 73.547
Unit cell angles	69.15, 68.93, 89.93

Refinement procedure

Resolution	50.000 - 2.100
R-factor	0.1946
Rwork	0.191
R-free	0.25970
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4qb0
RMSD bond length	0.007
RMSD bond angle	1.092
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0124)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.140
High resolution limit [Å]	2.100	5.700	2.100
Rmerge	0.070	0.038	0.316
Rmeas	0.096	0.052	0.436
Rpim	0.065	0.035	0.299
Total number of observations	103077
Number of reflections	48426
<I/σ(I)>	7.8
Completeness [%]	96.1	97.1	84.6
Redundancy	2.1	2.2	2
CC(1/2)		0.995	0.789

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.64	293	Crystallization conditions: 10% PEG 3350, 0.1 M Tris-HCl/HEPES pH 8.64. 1:1 ratio of precipitant solution to protein, with a protein concentration of 5.0 mg/mL. There was a 1.5 M NaCl alternative reservoir