1UA3

Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1996-04-20
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	69.781, 113.183, 116.924
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.000 * - 2.010
R-factor	0.1835
Rwork	0.175
R-free	0.19800 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007 *
RMSD bond angle	1.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000 *	2.040
High resolution limit [Å]	2.010	2.010
Rmerge	0.055	0.218
Total number of observations	211556 *
Number of reflections	61415 *
<I/σ(I)>	9.5	1.6
Completeness [%]	98.3	85.8
Redundancy	3.7	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.8 *	4 *	White, J.L., (1982) FEBS Lett., 148, 87. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	5 (mg/ml)
2	1	drop	potassium phosphate	50 (mM)
3	1	drop	EDTA	5 (mM)
4	1	drop	DTE	1-2 (mM)
5	1	drop	PEG10000	16-18 (%(w/v))
6	1	reservoir	PEG10000	32-36 (%(w/v))