7TAA

FAMILY 13 ALPHA AMYLASE IN COMPLEX WITH ACARBOSE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1995
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	51.040, 67.183, 133.560
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.980
R-factor	0.159 *
Rwork	0.159
R-free	0.23600
Structure solution method	NATIVE STRUCTURE
RMSD bond length	0.014
RMSD bond angle	0.033
Data reduction software	DENZO
Data scaling software	Agrovata
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.090
High resolution limit [Å]	1.980	1.980
Rmerge	0.088	0.291
Total number of observations	113411 *
Number of reflections	31062 *
<I/σ(I)>	12.6	5.1
Completeness [%]	97.0	94.2
Redundancy	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.5	18 *	18% MM PEG 5000, 5MM CALCIUM CHLORIDE, 0.1M HEPES BUFFER, PH 7.5. METHOD: HANGING DROP VAPOUR DIFFUSION. THE NATIVE CRYSTALS WERE SOAKED FOR 6 HOURS IN STABILIZING SOLUTION CONTAINING 15 MM OF ACARBOSE., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	HEPES-HCl	0.1 (M)
2	1	reservoir		5 (mM)
3	1	reservoir	mPEG5000 MW	16-18 (%(w/v))
4	1	drop	Tris-HCl	10 (mM)
5	1	drop		5 (mM)
6	1	drop	enzyme	30 (mg/ml)