1MVB

STRUCTURE OF A PROTEIN CAPSID OF THE T59S MUTANT OF PHAGE MS2

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	280
Detector technology	IMAGE PLATE
Collection date	1994-12
Detector	MARRESEARCH
Spacegroup name	H 3 2
Unit cell lengths	288.000, 288.000, 653.000
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 - 3.000
R-factor	0.173
Rwork	0.173
R-free	0.21800 *
Structure solution method	MIR
RMSD bond length	0.016
RMSD bond angle	27.500 *
Data reduction software	DENZO
Data scaling software	CCP4 ((AGROVATA)
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	3.200
High resolution limit [Å]	3.000	3.000
Rmerge	0.092 *	0.233 *
Number of reflections	128511 *	8748 *
<I/σ(I)>	7	3
Completeness [%]	61.8 *	58.3 *
Redundancy	1.7	2.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.4	37 *	1.5 % PEG 6000, 0.2 M SODIUM PHOSPHATE PH 7.4

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	MS2	1.0 (%(w/v))
2	1	drop	sodium phosphate	0.2 (M)
3	1	drop	PEG6000	1.5 (%(w/v))
4	1	drop		0.02 (%(w/v))
5	1	reservoir	sodium phosphate	0.4 (M)