1VCP

SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM I)

Experimental procedure

Detector technology	AREA DETECTOR
Detector	SIEMENS
Spacegroup name	P 1 21 1
Unit cell lengths	39.140, 176.220, 40.210
Unit cell angles	90.00, 110.36, 90.00

Refinement procedure

Resolution	6.000 - 3.000
R-factor	0.157
Rwork	0.157
RMSD bond length	0.013
RMSD bond angle	1.700
Data reduction software	XDS
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000 *
High resolution limit [Å]	3.000 *	3.000 *
Rmerge	0.076	0.118 *
Number of reflections	6747	1933 *
Completeness [%]	66.0	44.3 *
Redundancy	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.3 *		KHGI4 WAS REQUIRED TO OBTAIN BIG CRYSTALS. EACH OF THREE MONOMERS OF THE SEMLIKI FOREST VIRUS CORE PROTEIN BIND ONE MERCURY ATOM. THE HG ATOM FORMS A S-HG-S BOND WITH CYS 119 AND CYS 134. IN THE NATIVE STRUCTURE THERE IS A DISULFIDE BRIDGE BETWEEN CYS 119 AND CYS 134. THE S-HG DISTANCE WAS RESTRAINED TO 2.45 ANGSTROMS WHILE THE BOND ANGLE OF S-HG-S WAS RESTRAINED TO 180 DEGREES.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	drop		5 (mM)
3	1	drop	PEG8000	3-5 (%(w/v))
4	1	drop	Tris-HCl	100-150 (mM)
5	1	reservoir	PEG8000	6-10 (%(w/v))
6	1	reservoir	Tris-HCl	200-300 (mM)