1E3X

Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-05-15
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	53.000, 78.200, 240.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.900
R-factor	0.14 *
Rwork	0.140
R-free	0.20000
Structure solution method	MIR
RMSD bond length	0.011
RMSD bond angle	0.030
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.960
High resolution limit [Å]	1.920	1.920
Rmerge	0.120	0.190
Number of reflections	39302
<I/σ(I)>	13	7
Completeness [%]	99.0	98
Redundancy	4.6	3.4

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)