1GAI

GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE

Experimental procedure

Source type	ROTATING ANODE
Source details	SIEMENS
Temperature [K]	293
Detector technology	AREA DETECTOR
Collection date	1993-10-20
Detector	SIEMENS
Spacegroup name	P 21 21 21
Unit cell lengths	116.900, 104.400, 48.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.700
R-factor	0.147
Rwork	0.147
R-free	0.16700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	NATIVE GLOCOAMYLASE
RMSD bond length	0.008
RMSD bond angle	21.600 *
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]	30.000	1.800
High resolution limit [Å]	1.690	1.700 *
Rmerge	0.055	0.257
Total number of observations	298712 *
Number of reflections	64713 *
<I/σ(I)>	36.16	3.3
Completeness [%]	96.0	75 *
Redundancy	4.66	1.9

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)