1MI5

The crystal structure of LC13 TcR in complex with HLAB8-EBV peptide complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-C
Synchrotron site	APS
Beamline	14-BM-C
Temperature [K]	100
Detector technology	CCD
Collection date	2002-04-07
Detector	ADSC QUANTUM 4
Wavelength(s)	1
Spacegroup name	P 21 21 21
Unit cell lengths	56.490, 105.900, 144.500
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.500
R-factor	0.226
Rwork	0.226
R-free	0.28800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	the unliganded components
RMSD bond length	0.008 *
RMSD bond angle	1.440 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.091	0.451
Total number of observations	77349 *
Number of reflections	29027 *
<I/σ(I)>	12.1	2.4
Completeness [%]	92.9	95
Redundancy	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	PEG, ammonium acetate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	25 (%)	pH7.5
2	1	reservoir	ammonium acetate	0.2 (M)