1A43

STRUCTURE OF THE HIV-1 CAPSID PROTEIN DIMERIZATION DOMAIN AT 2.6A RESOLUTION

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X8C
Synchrotron site	NSLS
Beamline	X8C
Temperature [K]	300
Detector technology	IMAGE PLATE
Collection date	1997-09
Detector	MARRESEARCH
Spacegroup name	I 41
Unit cell lengths	60.410, 60.410, 60.430
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.600
R-factor	0.223
Rwork	0.223
R-free	0.28100
RMSD bond length	0.009
RMSD bond angle	21.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.843)
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.600
Rmerge	0.072 *	0.529 *
Total number of observations	21325 *
Number of reflections	3166 *
Completeness [%]	91.3 *	92.5 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5		drop contained 1:1 mixture of protein and reservoir solution *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.1 (mM)
2	1	drop	Tris-HCl	10 (mM)
3	1	drop	2-mercaptoethanol	2 (mM)
4	1	reservoir	ammonium sulfate	0.7 (M)
5	1	reservoir	lithium sulfate	1.0 (M)
6	1	reservoir	HEPES	0.1 (M)