1JAE

STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Detector technology	IMAGE PLATE
Detector	MAR scanner 300 mm plate
Spacegroup name	P 21 21 21
Unit cell lengths	51.240, 93.460, 96.950
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	7.000 - 1.650
R-factor	0.177
Rwork	0.177
R-free	0.20600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PIG PANCREATIC ALPHA AMYLASE
RMSD bond length	0.008
RMSD bond angle	1.482
Data reduction software	MOSFLM (V. 5.23)
Data scaling software	CCP4
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	1.650	1.640 *
Rmerge	0.057
Total number of observations	244244 *
Number of reflections	58219
Completeness [%]	99.9	99.2 *
Redundancy	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.4 *	22 *	Strobl, S., (1997) FEBS Lett., 409, 109. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	acetic acid/NaOH	5 (mM)
2	1	drop		0.1 (mM)
3	1	drop	protein	63 (mg/ml)
4	1	reservoir	sodium acetate	200 (mM)
5	1	reservoir	Bis-Tris-HCl	100 (mM)
6	1	reservoir	PEG8000	30 (%(w/v))