4RUN

Crystal structure of human odorant binding protein OBPIIa

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.2
Synchrotron site	BESSY
Beamline	14.2
Temperature [K]	100
Detector technology	CCD
Collection date	2011-12-07
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.9184
Spacegroup name	P 41 21 2
Unit cell lengths	52.949, 52.949, 232.098
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.700 - 2.600
R-factor	0.2373
Rwork	0.235
R-free	0.28440
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3eyc
RMSD bond length	0.008
RMSD bond angle	1.309
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	35.000	35.000	2.700
High resolution limit [Å]	2.600	10.000	2.600
Rmerge	0.049	0.016	0.645
Number of reflections	10926	240	1113
<I/σ(I)>	31.88	81	2.76
Completeness [%]	99.7	96.4	97.5
Redundancy	8.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	3.5	293	Protein solution: 14 mg/ml protein, 0.2 M imidazole, 0.4 M NaCl, 10 mM Tris-HCl, 1.3 mM Menthol, 3.3 %(v/v) Methanol; Reservoir solution: 20 %(w/v) PEG 3350, 0.1 M ammonium citrate, pH 3.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K