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EXTRACELLULAR DOMAIN OF THE 55KDA TUMOR NECROSIS FACTOR RECEPTOR. CRYSTALLIZED AT PH3.7 IN P 21 21 21.

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	123
Detector technology	IMAGE PLATE
Collection date	1994-03-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	78.810, 83.060, 67.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.850
R-factor	0.205 *
Rwork	0.203
R-free	0.24300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ncf
RMSD bond length	0.009
RMSD bond angle	25.290 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	11.000 *	1.930
High resolution limit [Å]	1.850 *	1.850
Rmerge	0.051
Number of reflections	37300 *
Completeness [%]	97.0	77
Redundancy	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	3.7	293 *	Rodseth, L.E., (1994) J.Mol.Biol., 239, 332. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	0.5 (mg/ml)
2	1	drop	PBS		0.025ml
3	1	drop	sodium formate	50 (mM)
4	1	drop		1 (M)
5	1	reservoir		1.7 (M)
6	1	reservoir	sodium formate	100 (mM)