1O8V

The crystal structure of Echinococcus granulosus fatty-acid-binding protein 1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	CCD
Collection date	2001-02-15
Detector	ADSC CCD
Spacegroup name	P 1 21 1
Unit cell lengths	28.714, 54.834, 38.691
Unit cell angles	90.00, 100.34, 90.00

Refinement procedure

Resolution	30.000 - 1.600
R-factor	0.174
Rwork	0.172
R-free	0.21400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1PMP CHAIN A
RMSD bond length	0.012
RMSD bond angle	1.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.100 *	1.660
High resolution limit [Å]	1.600	1.600
Rmerge	0.043	0.066
Total number of observations	81862 *
Number of reflections	15644
<I/σ(I)>	35	14.7
Completeness [%]	99.8	98.6
Redundancy	5.23

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8.3 *		30% (V/V) MMEPEG 5000, 0.1 M TRIS-HCL,PH 8.6,0.1 M NAAC.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris-HCl	30 (mM)	pH8.3
3	1	reservoir	PEG5000 MME	30 (%(v/v))
4	1	reservoir	Tris-HCl	0.1 (M)	pH8.6
5	1	reservoir	sodium acetate	0.1 (M)