1IEQ

CRYSTAL STRUCTURE OF BARLEY BETA-D-GLUCAN GLUCOHYDROLASE ISOENZYME EXO1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	MACSCIENCE
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-11-15
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 43 21 2
Unit cell lengths	100.951, 100.951, 181.196
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.700
R-factor	0.1887 *
Rwork	0.189
R-free	0.22840 *
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]	100.000	6.000
High resolution limit [Å]	2.700	2.700
Rmerge	0.117	0.421
Total number of observations	164280 *
Number of reflections	26752
<I/σ(I)>	7.7
Completeness [%]	99.9	99.9
Redundancy	6.16

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)