1AGB

ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGRKKYKL-3R MUTATION)

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	187
Detector technology	IMAGE PLATE
Collection date	1996-09-02
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	51.000, 81.600, 111.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.000 - 2.200
Rwork	0.195
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	HLA B27
RMSD bond length	0.012
RMSD bond angle	1.600
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	PROLSQ

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	14.000	2.300
High resolution limit [Å]	2.200	2.200
Rmerge	0.089	0.232
Total number of observations	88881 *
Number of reflections	27424
<I/σ(I)>	8.5
Completeness [%]	97.7	91.5
Redundancy	3.2

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)