4LUR

Crystal Structure of Zebrafish Interphotoreceptor Retinoid-Binding Protein (IRBP) Module 1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2009-02-25
Detector	ADSC QUANTUM 315
Wavelength(s)	0.979368, 0.979484, 0.9716932
Spacegroup name	P 21 21 2
Unit cell lengths	83.295, 97.771, 41.214
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.900
R-factor	0.222
Rwork	0.219
R-free	0.26800
Structure solution method	MAD COMBINED WITH MOLECULAR REPLACEMENT
Starting model (for MR)	1j7x
RMSD bond length	0.012
RMSD bond angle	1.374
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	CCP4
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.950
High resolution limit [Å]	1.900	1.901
Rmerge	0.085	0.640
Number of reflections	27277
<I/σ(I)>	40	2.8
Completeness [%]	99.6	99.8
Redundancy	6.8	6.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		7.5	295	Protein solutions at a concentration of 20mg/ml were mixed with the reservoir solutions of 35-44% polyethylene glycol 8000 in 100mM HEPES pH 7.5 buffer containing 100mM NaBr in the 1:1, 2:1 and 3:1 volume ratios and vapor diffused against the reservoir solutions. Plate-shaped crystals appeared in about a week and continued to grow for a few more weeks., VAPOR DIFFUSION, SITTING DROP, temperature 295.K