3VFR

crystal structure of HLA B*3508LPEP-P4Ala, peptide mutant P4-ala

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	2010-12-07
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9536
Spacegroup name	P 21 21 21
Unit cell lengths	50.340, 80.664, 109.664
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.833 - 1.850
R-factor	0.1781
Rwork	0.175
R-free	0.23170
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1zhk
RMSD bond length	0.007
RMSD bond angle	1.132
Data scaling software	SCALA (3.3.15)
Phasing software	PHASER
Refinement software	PHENIX (1.7.1_743)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	64.979	19.833	1.950
High resolution limit [Å]	1.850	5.850	1.850
Rmerge		0.035	0.444
Total number of observations		8775	40323
Number of reflections	38917
<I/σ(I)>	17.6	19.5	1.7
Completeness [%]	99.9	97.2	100
Redundancy	7.2	6.6	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	293	0.2M ammonium acetate, 16% PEG 4K, 0.1M sodium citrate pH5.6, vapor diffusion, hanging drop, temperature 293K