1AGF

ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKRYKL-5R MUTATION)

Experimental procedure

Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID2
Synchrotron site	ESRF
Beamline	ID2
Temperature [K]	187
Detector technology	CCD
Collection date	1995-07-25
Spacegroup name	P 21 21 21
Unit cell lengths	50.600, 81.300, 110.100
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.000 - 2.200
R-factor	0.181
Rwork	0.181
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	HLA B27
RMSD bond length	0.013
RMSD bond angle	1.700
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	14.000	2.300
High resolution limit [Å]	2.200	2.200
Rmerge	0.076 *	0.170
Total number of observations	140466 *
Number of reflections	26227
<I/σ(I)>	5.7
Completeness [%]	96.3	95.2
Redundancy	5.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8 *	21 *	Reid, S.W., (1996) Febs Lett., 383, 119. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris	20 (mM)
3	1	reservoir	PEG4000	30 (%)
4	1	reservoir	sodium citrate	0.1 (M)
5	1	reservoir	ammonium acetate	0.03 (M)