1A1M

MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
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	50.900, 82.500, 109.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.300
R-factor	0.205
Rwork	0.205
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hsa
RMSD bond length	0.014
RMSD bond angle	26.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall
Low resolution limit [Å]	15.000
High resolution limit [Å]	2.300
Rmerge	0.088
Number of reflections	27424
Completeness [%]	97.9
Redundancy	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.5	21 *	18% PEG8000 0.1M SODIUM CACODYLATE PH6.5 0.2M CALCIUM ACETATE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	calcium acetate	0.2 (M)
3	1	reservoir	sodium cacodylate	0.1 (M)	pH6.5
4	1	reservoir	PEG8000	18 (%)