1QH6

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	71.910, 74.830, 78.350
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.142 *
Rwork	0.142
R-free	0.18900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	0.029
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.030
High resolution limit [Å]	2.000	2.000
Rmerge	0.068	0.154
Number of reflections	27820
<I/σ(I)>	22.5	8.7
Completeness [%]	97.6	82.5
Redundancy	5.4	5.6

Crystallization Conditions

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

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 (%)