1KJ2

Murine Alloreactive ScFv TCR-Peptide-MHC Class I Molecule Complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	2000-02-19
Detector	MARRESEARCH
Wavelength(s)	0.987
Spacegroup name	P 1 21 1
Unit cell lengths	89.200, 77.920, 132.960
Unit cell angles	90.00, 108.23, 90.00

Refinement procedure

Resolution	12.000 - 2.710
R-factor	0.219
Rwork	0.220
R-free	0.27800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1kb5 1kj3
RMSD bond length	0.009
RMSD bond angle	1.600 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	14.990	2.850
High resolution limit [Å]	2.700 *	2.710
Rmerge	0.084 *
Number of reflections	45992
<I/σ(I)>	7.7	2
Completeness [%]	96.9	87.8
Redundancy	3.4	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.7	20 *	17-19% PEG 6000, 0.1M Mes, 0.1M NaCl, 0.1M MgAc, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	4.0 (mg/ml)
2	1	reservoir	PEG6000	17-19 (%)
3	1	reservoir	MES	0.1 (M)	pH6.7
4	1	reservoir		0.1 (M)
5	1	reservoir		0.1 (M)