1OA2

Comparison of Family 12 Glycoside Hydrolases and Recruited Substitutions Important for Thermal Stability

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2000-12-03
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	68.280, 71.290, 119.300
Unit cell angles	90.00, 91.49, 90.00

Refinement procedure

Resolution	20.000 - 1.500
R-factor	0.20557
Rwork	0.205
R-free	0.21900 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1h8v
RMSD bond length	0.018 *
RMSD bond angle	1.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.530
High resolution limit [Å]	1.500	1.500
Rmerge	0.037 *	0.381 *
Total number of observations	490560 *
Number of reflections	172895
<I/σ(I)>	24.9	3
Completeness [%]	94.4 *	94.3 *
Redundancy	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6	20-24 *	pH 6.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	cacodylate	200 (mM)	pH6.0
2	1	reservoir	calcium acetate	200 (mM)
3	1	reservoir	PEG2000MME	10-30 (%(w/w))
4	1	drop	protein	20 (mg/ml)