1J12

Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	177.900, 112.900, 146.200
Unit cell angles	90.00, 105.80, 90.00

Refinement procedure

Resolution	8.000 - 2.100
Rwork	0.198
R-free	0.25300
Starting model (for MR)	5bca
RMSD bond length	0.007
RMSD bond angle	21.965 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	73.400	2.090
High resolution limit [Å]	2.000	2.000
Rmerge	0.087	0.247
Total number of observations	257638 *
Number of reflections	128094	6376 *
Completeness [%]	68.6	27.4
Redundancy	2.0 *	1.2 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	9	293	Oyama, T., (1998) Protein Pept.Lett., 5, 349. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	ammonium chloride	50 (mM)
3	1	reservoir	PEG6000	6-8 (%(w/v))
4	1	reservoir	ammonium chloride	50 (mM)