7KD4

Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P21.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Synchrotron site	Australian Synchrotron
Beamline	MX1
Temperature [K]	110
Detector technology	CCD
Collection date	2016-10-10
Detector	ADSC QUANTUM 210
Wavelength(s)	0.9537
Spacegroup name	P 1 21 1
Unit cell lengths	57.561, 70.074, 111.739
Unit cell angles	90.00, 96.47, 90.00

Refinement procedure

Resolution	59.329 - 1.312
Rwork	0.150
R-free	0.19570
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4kyc
RMSD bond length	0.009
RMSD bond angle	1.454
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.8.0230 2018/03/05)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	59.330	1.330
High resolution limit [Å]	1.310	1.310
Rmerge	0.051	0.607
Rmeas	0.061	0.857
Rpim	0.032	0.605
Number of reflections	149703	307
<I/σ(I)>	10.9
Completeness [%]	70.7	2.9
Redundancy	3.2	1.5
CC(1/2)		0.783

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	291.15	1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, Crystals were transferred into the following cryo-protective solution before vitrification: 1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, 5mM Maltose, 1 M Lithium sulfate