1E43

Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	1999-09-15
Detector	ADSC-Q4
Spacegroup name	C 2 2 21
Unit cell lengths	52.200, 76.100, 236.500
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.700
R-factor	0.133 *
Rwork	0.133
R-free	0.18500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1e3x
RMSD bond length	0.010
RMSD bond angle	0.026
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.070	0.081
Number of reflections	51292
<I/σ(I)>	15	13
Completeness [%]	98.0	99
Redundancy	3	3.1

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.

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)