1E40

Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1994-10-15
Detector	RAXIS IIC
Spacegroup name	C 2 2 21
Unit cell lengths	52.720, 78.270, 238.860
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.200
R-factor	0.13 *
Rwork	0.130
R-free	0.21000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1e3x
RMSD bond length	0.010
RMSD bond angle	0.030
Data reduction software	DENZO
Data scaling software	Agrovata
Phasing software	CCP4
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.300
High resolution limit [Å]	2.200	2.200
Rmerge	0.050	0.089 *
Number of reflections	23662
<I/σ(I)>	33	13
Completeness [%]	94.0	77
Redundancy	5.2	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	18 *	CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML. CRYSTALS WERE THEN SOAKED IN 10MM MALTOTRIOSE SOLUTION TO OBTAIN THE COMPLEX.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	mmePEG2000	8-13 (%(w/v))	or PEG5000
2	1	drop	Tris-HCl	0.1 (M)
3	1	drop		5 (mM)
4	1	drop	protein	30-35 (M)