1DLB

HELICAL INTERACTIONS IN THE HIV-1 GP41 CORE REVEALS STRUCTURAL BASIS FOR THE INHIBITORY ACTIVITY OF GP41 PEPTIDES

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1999-03-11
Detector	RIGAKU RAXIS IV
Spacegroup name	H 3
Unit cell lengths	52.382, 52.382, 60.482
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 - 2.000
R-factor	0.206
Rwork	0.206
R-free	0.24300
RMSD bond length	0.005
RMSD bond angle	0.800
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.5)

Data quality characteristics

	Overall
Low resolution limit [Å]	50.000
High resolution limit [Å]	2.000
Rmerge	0.040
Total number of observations	23565 *
Number of reflections	4167
Completeness [%]	99.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	4.6	293	PEG 4000, AMMONIUM SULPHATE, SODIUM ACETATE, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	peptide	10 (mg/ml)
2	1	reservoir	ammonium sulfate	0.2 (M)
3	1	reservoir	sodium acetate	0.1 (M)	pH4.6
4	1	reservoir	PEG4000	11 (%)