1HV0

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	1999-05-01
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	44.055, 52.695, 78.538
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.600
R-factor	0.181 *
Rwork	0.181
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bcx
RMSD bond length	0.006
RMSD bond angle	1.150
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 *	1.660
High resolution limit [Å]	1.600	1.600
Rmerge	0.048	0.162
Total number of observations	157188 *
Number of reflections	24862
<I/σ(I)>	28
Redundancy	6.3

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)