5A2C

Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2014-07-10
Detector	RIGAKU R-AXIS IV
Spacegroup name	P 21 21 21
Unit cell lengths	61.816, 63.532, 122.970
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	61.490 - 1.900
R-factor	0.1585
Rwork	0.156
R-free	0.20914
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4e2o
RMSD bond length	0.018
RMSD bond angle	1.821
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.540	1.940
High resolution limit [Å]	1.900	1.900
Rmerge	0.090	0.580
Number of reflections	37601
<I/σ(I)>	12.6	1.9
Completeness [%]	96.7	86.6
Redundancy	3.6	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		6.5		THE TASKA-MALTODP3 NAMELY TASKA-T COMPLEXES WAS CRYSTALLIZED USING THE STREAK SEEDING METHOD WITH A COMMERCIALLY AVAILABLE SEEDING TOOL, HAMPTON RESEARCH, USA. THE SEEDING TOOL WAS DIPPED INTO A DROP CONTAINING TASKA-APO,PDB ID 5A2A, CRYSTALS AND STREAKED ON THE DROPS THAT CONSISTED OF 0.3 UL 6 MG/ML TASKA PROTEIN AND 0.3 UL RESERVOIR SOLUTION 0.1 M CALCIUM ACETATE, 0.1 M SODIUM CACODYLATE PH 6.5, AND 18 % W/V POLYETHYLENE GLYCOL 8,000 WITH 20 MM MALTOTRIOSE.