1OA4

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-02-15
Detector	MSC
Spacegroup name	P 21 21 21
Unit cell lengths	65.160, 54.630, 62.590
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.000 - 1.500
R-factor	0.18185
Rwork	0.181
R-free	0.19300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nlr
RMSD bond length	0.012 *
RMSD bond angle	1.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.000	1.530
High resolution limit [Å]	1.500	1.500
Rmerge	0.054 *	0.161 *
Total number of observations	88448 *
Number of reflections	26559
<I/σ(I)>	15.4	8.6
Completeness [%]	72.9 *	63.5
Redundancy	3.3 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6	25 *	pH 6.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG5000 MME	10-20 (%(w/w))
2	1	reservoir	sodium cacodylate	200 (mM)	pH5.0-6.0
3	1	drop	protein	15 (mg/ml)