7KD5

Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P212121

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	2016-09-19
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	67.617, 77.421, 79.132
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	31.240 - 1.551
Rwork	0.164
R-free	0.18870
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4kyc
RMSD bond length	0.007
RMSD bond angle	1.529
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.8.0266)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.300	1.570
High resolution limit [Å]	1.540	1.540
Rmerge	0.024	0.186
Rmeas	0.026	0.204
Rpim	0.010	0.081
Number of reflections	59991	2017
<I/σ(I)>	44.63
Completeness [%]	97.4	66.5
Redundancy	6.8	5.6
CC(1/2)		0.982

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.7	291.15	20%(w/v) PEG 5000 mono-methyl ether, 0.2 M Pipes/KOH pH 6.7, 0.1M Proline, Crystals were transferred into the following cryo-protective solution before vitrification: 20%(w/v) PEG 5000 mono-methyl ether, 0.2 M Pipes/KOH pH 6.7, 0.1M Proline, 5mM Maltose, 20%(v/v) Ethylene Glycol