1HT6

CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-05-17
Detector	MARRESEARCH
Wavelength(s)	0.9761
Spacegroup name	P 21 21 2
Unit cell lengths	88.360, 72.820, 61.740
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.600 * - 1.500
Rwork	0.136
R-free	0.16300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	AMY1 structure solved at 2.0A resolution (unpublished results)
RMSD bond length	0.017
RMSD bond angle	1.700
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	41.600	1.540
High resolution limit [Å]	1.500	1.500
Rmerge	0.045	0.119
Total number of observations	271695 *
Number of reflections	63366
<I/σ(I)>	13.3	6.2
Completeness [%]	98.7	97.3
Redundancy	4.3	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.7	290 *	Robert, X., (2002) Acta Crystallogr., D58, 683. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.1 (mg/ml)
2	1	drop	2-propanol	3 (%(v/v))
3	1	reservoir	PEG8000	20 (%(w/v))