1QH7

CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-05-01
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	71.860, 75.360, 78.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.780
R-factor	0.117 *
Rwork	0.117
R-free	0.17600
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	0.031
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	54.200	1.810
High resolution limit [Å]	1.780	1.780
Rmerge	0.055	0.162
Number of reflections	40782
<I/σ(I)>	27.4	6.7
Completeness [%]	99.1	98.3
Redundancy	5.6	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6 *		AMMONIUM SULPHATE 30%, MES 0.1M PH 6.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	sodium acetate	100 (mM)
3	1	reservoir	MES	100 (mM)
4	1	reservoir	ammonium sulfate	30 (%)