3KWW

Crystal structure of the 'restriction triad' mutant of HLA B*3508, beta-2-microglobulin and EBV peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Synchrotron site	Australian Synchrotron
Beamline	MX1
Temperature [K]	298
Collection date	2008-05-12
Spacegroup name	P 21 21 21
Unit cell lengths	50.972, 81.454, 110.380
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.670 - 2.180
R-factor	0.188
Rwork	0.186
R-free	0.25100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1zhl
RMSD bond length	0.007
RMSD bond angle	1.040
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.260
High resolution limit [Å]	2.180	2.180
Rmerge	0.057
Number of reflections	24588
<I/σ(I)>	16.7	3.8
Completeness [%]	99.4	99.9
Redundancy	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.6	298	0.1M cacodlyate, 0.2M ammonium acetate, 18% PEG3350, pH 7.6, vapor diffusion, temperature 298K