1DL7

THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	298
Spacegroup name	P 21 21 21
Unit cell lengths	130.900, 35.900, 50.450
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.350
R-factor	0.191
Rwork	0.189
R-free	0.26500
RMSD bond length	0.014
RMSD bond angle	1.900
Data reduction software	bioteX
Data scaling software	bioteX
Phasing software	EPMR
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000	2.420
High resolution limit [Å]	2.350	2.350
Rmerge	0.073	0.265 *
Total number of observations	47930 *
Number of reflections	8983
<I/σ(I)>	8.5
Completeness [%]	84.0	47 *
Redundancy	2	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.5	298	SODIUM/POTASSIUM PHOSPHATE, HEPES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.6 (mg/ml)
2	1	drop	NPPC	2 (mM)
3	1	reservoir		1.5 (M)
4	1	reservoir	HEPES	0.1 (M)