1H2C

Ebola virus matrix protein VP40 N-terminal domain in complex with RNA (High-resolution VP40[55-194] variant).

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Spacegroup name	P 4 2 2
Unit cell lengths	80.510, 80.510, 46.770
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 1.600
R-factor	0.165
Rwork	0.164
R-free	0.18200
Structure solution method	MAD
RMSD bond length	0.008 *
RMSD bond angle	1.180 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000
High resolution limit [Å]	1.600
Rmerge	0.065	0.341 *
Total number of observations	167556 *
Number of reflections	19961 *
<I/σ(I)>	7.1
Completeness [%]	95.9	78.2 *
Redundancy	8.4	2.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5		1 UL OF PROTEIN SOLUTION (10 MG/ML) AND 1 UL OF WELL SOLUTION (100 MM HEPES PH 7.5, 1.5 M NH4H2PO4,15 % MPD). HANGING DROP.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	HEPES	100 (mM)	pH7.5
3	1	reservoir		1.5 (M)
4	1	reservoir	MPD	15 (%)