2XGB

Crystal structure of Barley Beta-Amylase complexed with 2,3- epoxypropyl-alpha-D-glucopyranoside

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX10.1
Synchrotron site	SRS
Beamline	PX10.1
Temperature [K]	100
Detector technology	CCD
Collection date	2007-11-12
Detector	MARMOSAIC 225 mm CCD
Spacegroup name	P 21 21 21
Unit cell lengths	68.622, 71.068, 92.309
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.168 - 1.200
R-factor	0.118
Rwork	0.117
R-free	0.14070
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1b1y
RMSD bond length	0.016
RMSD bond angle	1.651
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.5.0091)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.690	1.260
High resolution limit [Å]	1.110	1.200
Rmerge	0.100	0.270
Number of reflections	135507
<I/σ(I)>	3.56	2.76
Completeness [%]	96.3	79.5
Redundancy	5.98	3.01

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	291	CRYSTALS WERE GROWN AT 291 K USING THE HANGING DROP VAPOUR DIFFUSION METHOD WITH PROTEIN AT 10 MG PER ML AND A PRECIPITANT COMPRISED OF 14 PERCENT PEG 3350 IN 100 MM BIS-TRIS PROPANE BUFFER AT PH 5.5