2F53

Directed Evolution of Human T-cell Receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without apparent cross-reactivity

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX14.1
Synchrotron site	SRS
Beamline	PX14.1
Temperature [K]	100
Detector technology	CCD
Collection date	2004-05-13
Detector	ADSC QUANTUM 4
Wavelength(s)	1.488
Spacegroup name	P 1 21 1
Unit cell lengths	76.234, 53.972, 119.905
Unit cell angles	90.00, 96.83, 90.00

Refinement procedure

Resolution	37.850 - 2.100
R-factor	0.169
Rwork	0.166
R-free	0.23110
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2bnr
RMSD bond length	0.014
RMSD bond angle	1.536
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE (CCP4 5.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	37.850	37.710	2.110
High resolution limit [Å]	2.000	6.320	2.000
Rmerge	0.178	0.011	0.011
Number of reflections	64982
<I/σ(I)>	3	5.9	0.5
Completeness [%]	98.7	98.7	97.4
Redundancy	10.4	9.5	9.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	85 mM HEPES, 8.5% Iso-propanol, 17% PEG4000, 15% glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K