1HV1

DISSECTING ELECTROSTATIC INTERACTIONS AND THE PH-DEPENDENT ACTIVITY OF A FAMILY 11 GLYCOSIDASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1999-10-01
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	43.994, 52.711, 78.202
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.800
R-factor	0.164
Rwork	0.164
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bcx
RMSD bond length	0.009
RMSD bond angle	0.911
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 *	1.880
High resolution limit [Å]	1.800	1.800
Rmerge	0.054	0.115
Total number of observations	157188 *
Number of reflections	17548
<I/σ(I)>	21.8
Redundancy	9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	Sidhu, G., (1999) Biochemistry, 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)