3CPU

SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	298
Detector technology	AREA DETECTOR
Spacegroup name	P 21 21 21
Unit cell lengths	52.910, 75.390, 136.120
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.000
R-factor	0.179
Rwork	0.179
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.330
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000
High resolution limit [Å]	2.000	2.000 *
Rmerge	0.079
Total number of observations	119912 *
Number of reflections	31361
Completeness [%]	83.4
Redundancy	3.8	1.6 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		pH 7.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	MPD	60 (%)
2	1	reservoir	cacodylate	100 (mM)
3	1	drop	protein	2 (mg/ml)