1QI5

MUTANT (D294N) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	65.720, 170.900, 46.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.000
R-factor	0.185
Structure solution method	OTHER
Starting model (for MR)	1jdd
RMSD bond length	0.014
RMSD bond angle	0.033
Phasing software	PHASER
Refinement software	PROFFT

Data quality characteristics

	Overall
Low resolution limit [Å]	45.000
High resolution limit [Å]	2.000
Rmerge	0.076
Total number of observations	110249 *
Number of reflections	31308
Completeness [%]	84.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	20 *	pH 7.5 THE CRYSTAL WAS SOAKED IN A SOLUTION OF 10 MG/ML MALTOPENTAOSE DURING DATA COLLECTION.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	14 (mg/ml)
2	1	drop	Tris/HCl	20 (mM)
3	1	drop	ammonium sulfate	0.7-0.9 (M)
4	1	drop	maltopentaose	10 (mg/ml)