Crystallization and preliminary X-ray study of minor glucoamylase from Aspergillus awamori variant X-100/D27

A M Golubev; K N Neustroev; A E Aleshin; L M Firsov

doi:10.1016/0022-2836(92)90139-b

Crystallization and preliminary X-ray study of minor glucoamylase from Aspergillus awamori variant X-100/D27

J Mol Biol. 1992 Jul 5;226(1):271-2. doi: 10.1016/0022-2836(92)90139-b.

Authors

A M Golubev¹, K N Neustroev, A E Aleshin, L M Firsov

Affiliation

¹ Leningrad Nuclear Physics Institute, U.S.S.R. Academy of Sciences, Gatchina.

PMID: 1619656
DOI: 10.1016/0022-2836(92)90139-b

Abstract

Crystals of the reduced form of glucoamylase were obtained from polyethylene glycol 6000 solution by the hanging-drop method. The protein was treated with alpha-mannosidase to partly remove the sugar component. The crystals belong to the space group P2(1)2(1)2(1) with cell dimensions a = 116.7 A, b = 104.3 A, c = 48.5 A and diffract beyond 2.5 A resolution.

MeSH terms

Aspergillus / enzymology*
Crystallization
Glucan 1,4-alpha-Glucosidase / chemistry*
Glucan 1,4-alpha-Glucosidase / metabolism
Mannosidases / metabolism
Polyethylene Glycols
X-Ray Diffraction
alpha-Mannosidase

Substances

Polyethylene Glycols
Mannosidases
alpha-Mannosidase
Glucan 1,4-alpha-Glucosidase