1A9E

DECAMER-LIKE CONFORMATION OF A NANO-PEPTIDE BOUND TO HLA-B3501 DUE TO NONSTANDARD POSITIONING OF THE C-TERMINUS

Experimental procedure

Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1997-05
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	45.510, 181.510, 141.150
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 - 2.500
R-factor	0.213
Rwork	0.213
R-free	0.26000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hhi
RMSD bond length	0.006
RMSD bond angle	25.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.075 *
Total number of observations	71576 *
Number of reflections	20331
<I/σ(I)>	16.2	4.2
Completeness [%]	98.5	99.3
Redundancy	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.9	18 *	4 M SODIUM FORMATE, PH 7.9

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7 (mg/ml)
2	1	reservoir	sodium formate	4 (M)