3SKM

Crystal structure of the HLA-B8FLRGRAYVL, mutant G8V of the FLR peptide

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	2011-03-31
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.954
Spacegroup name	P 21 21 21
Unit cell lengths	50.720, 81.680, 112.070
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.885 - 1.800
R-factor	0.1771
Rwork	0.175
R-free	0.21200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1m05
RMSD bond length	0.006
RMSD bond angle	1.033
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.6.1_357)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	100.000	100.000	1.900
High resolution limit [Å]	1.800	10.000	1.800
Rmerge	0.097	0.038	0.570
Number of reflections	43886	261	6457
<I/σ(I)>	16.46	35.8	4.85
Completeness [%]	99.9	84.7	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	277	0.2M ammonium acetate, 20% PEG 4000, 0.1M tri-Na citrate, pH 5.6, vapor diffusion, hanging drop, temperature 277K