1B2Y

STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Temperature [K]	293
Collection date	1998-07-15
Spacegroup name	P 21 21 21
Unit cell lengths	53.110, 75.100, 137.130
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	11.000 - 3.200
R-factor	0.191
Rwork	0.191
R-free	0.21700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hny
RMSD bond length	0.015
RMSD bond angle	1.900
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	3.270
High resolution limit [Å]	3.200	3.200
Rmerge	0.158	0.286
Total number of observations	45084 *
Number of reflections	10103
<I/σ(I)>	9.2	5.7
Completeness [%]	91.8	63.4
Redundancy	4.4	9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8		60% 2-METHYLPENTAN-2,4 DIOL, pH 8.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	18 (mg/ml)
2	1	reservoir	MES	0.1 (M)
3	1	reservoir	MPD	55 (%(v/v))