1BG9

BARLEY ALPHA-AMYLASE WITH SUBSTRATE ANALOGUE ACARBOSE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	288
Detector technology	AREA DETECTOR
Collection date	1992-04
Detector	SIEMENS
Spacegroup name	P 31 2 1
Unit cell lengths	135.200, 135.200, 79.600
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 - 2.800
R-factor	0.151
Rwork	0.151
R-free	0.24900
Structure solution method	REFINEMENT DIFFERENCE FOURIER
Starting model (for MR)	1amy
RMSD bond length	0.015 *
RMSD bond angle	23.600 *
Data reduction software	XENGEN ((HOWARD)
Data scaling software	XENGEN
Phasing software	X-PLOR (2.1)
Refinement software	X-PLOR (2.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]		2.900
High resolution limit [Å]	2.729	2.729
Rmerge	0.092	0.270
Total number of observations	61039 *
Number of reflections	17688
<I/σ(I)>	16.6	1.7
Completeness [%]	90.5	44.8
Redundancy	2.9	1.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.7		Svensson, B., (1987) J. Biol. Chem., 262, 13682. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop		1 (mM)
2	1	drop	MES	10 (mM)
3	1	drop	protein	4-16 (mg/ml)
4	1	reservoir	ammonium sulfate	10 (%sat)