1GAH

GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE

Experimental procedure

Source type	ROTATING ANODE
Source details	SIEMENS
Temperature [K]	293
Detector technology	AREA DETECTOR
Detector	SIEMENS
Spacegroup name	P 21 21 21
Unit cell lengths	116.800, 104.100, 48.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.000
R-factor	0.131
Rwork	0.131
R-free	0.15900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	NATIVE GLUCOAMYLASE
RMSD bond length	0.008
RMSD bond angle	21.500 *
Data reduction software	XENGEN
Data scaling software	XENGEN
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.130
High resolution limit [Å]	2.000	2.000
Rmerge	0.057	0.145
Total number of observations	87952 *
Number of reflections	34394
<I/σ(I)>	22	5.6
Completeness [%]	85.0 *	54 *
Redundancy	2.56	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5 *		Golubev, A. M., (1992) J. Mol. Biol., 226, 271. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-15 (mg/ml)
2	1	drop	PEG6000	30 (%(w/v))
3	1	drop	sodium phosphate	0.15 (M)
4	1	reservoir	PEG6000	30 (%(w/v))
5	1	reservoir	sodium phosphate	0.15 (M)