1C28

THE CRYSTAL STRUCTURE OF A COMPLMENT-1Q FAMILY PROTEIN SUGGESTS AN EVOLUTIONARY LINK TO TUMOR NECROSIS FACTOR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	1997-01-01
Detector	RIGAKU RAXIS
Spacegroup name	P 61
Unit cell lengths	112.300, 112.300, 71.600
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.100
R-factor	0.212
Rwork	0.212
R-free	0.27600
RMSD bond length	0.012
RMSD bond angle	1.899
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	8.000	2.170
High resolution limit [Å]	2.100	2.100
Rmerge	0.091	0.199
Number of reflections	27888
<I/σ(I)>	12.05
Completeness [%]	92.8	92.2
Redundancy	3	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	4. *	1.8% PEG 4K, 0.1M BIS-TRIS, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 4.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	PEG4000	1.8 (%)
3	1	reservoir	Bis-Tris	0.1 (M)