1QMT

Recombinant Human Eosinophil Cationic Protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1999-03-15
Detector	MARRESEARCH
Spacegroup name	P 63
Unit cell lengths	100.159, 100.159, 31.281
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.400
R-factor	0.176
Rwork	0.176
R-free	0.22900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	EOSINOPHIL DERIVED NEUROTOXIN STRUCTURE AT 1.8 ANGSTROMS (COORDINATES NOT SUBMITTED) WAS PROVIDED BY S.MOSIMANN AND M.N.G.JAMES AND USED FOR MOLECULAR REPLACEMENT.
RMSD bond length	0.010
RMSD bond angle	28.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.107	0.287
Total number of observations	34137 *
Number of reflections	6916
<I/σ(I)>	10.7	3.5
Completeness [%]	95.7	65
Redundancy	4.93

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8	16 *	microseeding *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	13 (mg/ml)
2	1	reservoir		0.5 (M)
3	1	reservoir	2-propanol	10 (%)
4	1	reservoir	HEPES	0.1 (M)