2W2S

Structure of the Lagos bat virus matrix protein

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	CCD
Collection date	2006-11-04
Detector	MARRESEARCH
Spacegroup name	P 61 2 2
Unit cell lengths	56.870, 56.870, 187.910
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	38.720 - 2.750
R-factor	0.21
Rwork	0.207
R-free	0.25500
Structure solution method	MAD
Starting model (for MR)	NONE
RMSD bond length	0.009
RMSD bond angle	1.093
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	autoSHARP
Refinement software	REFMAC (5.4.0077)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.720	2.820
High resolution limit [Å]	2.750	2.750
Rmerge	0.130	0.770
Number of reflections	5164
<I/σ(I)>	10.2	2.2
Completeness [%]	99.6	99.4
Redundancy	6.2	5.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4		SITTING DROPS CONTAINING 100 NL OF 1.1 MG/ML PROTEIN AND 100 NL OF RESERVOIR SOLUTION (100 MM CITRATE PH 4.0 AND 10%(W/V) POLYETHYLENE GLYCOL (PEG) 6000) WERE EQUILIBRATED AGAINST 95 UL RESERVOIRS AT 20.5C. CRYSTALS WERE CRYOPROTECTED BY BRIEF IMMERSION IN RESERVOIR SOLUTION SUPPLEMENTED WITH 25% V/V GLYCEROL.