1UCT

Crystal structure of the extracellular fragment of Fc alpha Receptor I (CD89)

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL41XU
Synchrotron site	SPring-8
Beamline	BL41XU
Temperature [K]	100
Detector technology	CCD
Collection date	2003-03-29
Detector	MARRESEARCH
Wavelength(s)	0.9000, 0.9798, 0.9800
Spacegroup name	C 2 2 21
Unit cell lengths	59.010, 69.450, 106.350
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 2.100
R-factor	0.222
Rwork	0.210
R-free	0.23900
Structure solution method	MAD
RMSD bond length	0.015
RMSD bond angle	1.800
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.061 *	0.234 *
Total number of observations	95489 *
Number of reflections	13108 *
Completeness [%]	100.0 *	99.9 *
Redundancy	7.3	7.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.6 *	291	PEG4000, sodium citrate, ethanol glycol, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	11.4 (%)
2	1	reservoir	sodium HEPES	100 (mM)	pH7.6
3	1	reservoir	ethylene glycol	8 (%(v/v))
4	1	reservoir		3 (%(v/v))
5	1	reservoir		50 (mM)
6	1	drop	protein	12 (mg/ml)