1LQ2

Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with gluco-phenylimidazole

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	MACSCIENCE
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-08-15
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 43 21 2
Unit cell lengths	100.693, 100.693, 182.676
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 - 2.620 *
Rwork	0.210
R-free	0.27290 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ieq
RMSD bond length	0.010
RMSD bond angle	1.700
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.690
High resolution limit [Å]	2.620	2.620
Rmerge	0.130	0.583 *
Total number of observations	70377 *
Number of reflections	44625 *
<I/σ(I)>	5.9
Completeness [%]	73.6 *	45.4 *
Redundancy	1.81

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)