4N1C

Structural evidence for antigen receptor evolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	100
Detector technology	CCD
Collection date	2012-03-01
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.95369
Spacegroup name	P 63
Unit cell lengths	126.789, 126.789, 40.660
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	41.500 - 1.700
R-factor	0.1986
Rwork	0.197
R-free	0.23250
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB entries 3UPA and 1ZVY
RMSD bond length	0.013
RMSD bond angle	1.385
Data reduction software	MOSFLM (3.3.16)
Data scaling software	SCALA (3.3.16)
Phasing software	PHASER (2.3.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	109.800	41.502	1.790
High resolution limit [Å]	1.700	5.380	1.700
Rmerge		0.051	0.575
Total number of observations		13805	38675
Number of reflections	41399
<I/σ(I)>	12.9	10.7	1.3
Completeness [%]	99.8	99	99.5
Redundancy	7.9	10	6.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	293	0.2 M ammonium acetate, 0.1 M BisTris (pH 5.5), 25% PEG3350, vapor diffusion, sitting drop, temperature 293K, VAPOR DIFFUSION, SITTING DROP