1AC6

CRYSTAL STRUCTURE OF A VARIABLE DOMAIN MUTANT OF A T-CELL RECEPTOR ALPHA CHAIN

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	293
Detector technology	AREA DETECTOR
Collection date	1995-11
Detector	SIEMENS
Spacegroup name	P 21 21 21
Unit cell lengths	72.430, 64.820, 45.540
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.300
R-factor	0.161
Rwork	0.161
R-free	0.27900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	VALPHA WILDTYPE HOMODIMER STRUCTURE OF 1934.4 TCR
RMSD bond length	0.011
RMSD bond angle	26.800 *
Data reduction software	XENGEN21
Data scaling software	XENGEN (V. 2.1)
Phasing software	AMoRE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.410	2.370
High resolution limit [Å]	2.120	2.300
Rmerge	0.105	0.406
Total number of observations	26767 *
Number of reflections	9957
<I/σ(I)>	6	1.38
Completeness [%]	78.2	72.7 *
Redundancy	3	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.7		PROTEIN WAS CRYSTALLIZED FROM 5.0M SODIUM FORMATE, PH 7.7 IN HANGING DROPS AT ROOM TEMPERATURE., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3.5 (mg/ml)
2	1	drop	sodium formate	2.50 (M)
3	1	reservoir	sodium formate	5.0 (M)