1C5H

HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	298
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	44.050, 52.690, 78.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.550
R-factor	0.194
Rwork	0.194
RMSD bond length	0.007
RMSD bond angle	1.210
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	9999.000 *
High resolution limit [Å]	1.550	1.550 *
Rmerge	0.057	0.152 *
Total number of observations	150984 *
Number of reflections	27301
<I/σ(I)>	21.1
Completeness [%]	99.9
Redundancy	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		Sidhu, G., (1999) J. Mol. Biol., 38, 5346. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	ammonium sulfate	17 (%)
3	1	reservoir		10 (mM)
4	1	reservoir	Tris-HCl	40 (mM)