1A1N

MHC CLASS I MOLECULE B*3501 COMPLEXED WITH PEPTIDE VPLRPMTY FROM THE NEF PROTEIN (75-82) OF HIV1

Experimental procedure

Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM1A
Synchrotron site	ESRF
Beamline	BM1A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-02-09
Detector	MAR scanner 300 mm plate
Spacegroup name	P 21 21 21
Unit cell lengths	50.000, 80.500, 105.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.000
R-factor	0.203
Rwork	0.203
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hsa
RMSD bond length	0.013
RMSD bond angle	26.490 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
Low resolution limit [Å]	10.000
High resolution limit [Å]	2.000
Rmerge	0.076
Total number of observations	177209 *
Number of reflections	32001
Completeness [%]	95.2
Redundancy	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.5	21 *	used to seeding *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	drop	sodium cacodylate	25 (mM)
3	1	reservoir	sodium cacodylate	0.1 (M)
4	1	reservoir	PEG8000	18 (%)