1CPU

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
Temperature [K]	298
Spacegroup name	P 21 21 21
Unit cell lengths	52.910, 68.900, 131.770
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.000
R-factor	0.17
Rwork	0.170
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.231
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	0.036
Total number of observations	157746 *
Number of reflections	33610
Completeness [%]	93.8
Redundancy	4.7	2.8 *

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)