1IEW

Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 2-deoxy-2-fluoro-alpha-D-glucoside

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	MACSCIENCE
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-11-23
Detector	RIGAKU RAXIS II
Wavelength(s)	1.5418
Spacegroup name	P 43 21 2
Unit cell lengths	100.962, 100.962, 181.254
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.550
R-factor	0.1889 *
Rwork	0.189
R-free	0.23310 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ex1
RMSD bond length	0.010
RMSD bond angle	1.300
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	15.000
High resolution limit [Å]	2.550	2.550
Rmerge	0.138	0.496
Total number of observations	283040 *
Number of reflections	30853
<I/σ(I)>	7.2
Completeness [%]	99.6	96.8
Redundancy	9.48

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	277-279 *	Hrmova, M., (1998) Acta Cryst., D54, 687. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	6.8 (mg/ml)
2	1	drop	HEPES-NaOH	75 (mM)
3	1	drop	sodium acetate	7.5 (mM)
4	1	drop	PEG400	1.2 (%(w/v))
5	1	drop	ammonium sulfate	0.8 (M)
6	1	reservoir	ammonium sulfate	1.7 (M)
7	1	reservoir	HEPES-NaOH	50 (mM)