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Title 

Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens

Authors 

Nam Chul HaYoung Ok KimTae Kwang OhByung Ha Oh

Publisher 

International Union of Crystallography

Issue Date 

1999

Citation 

Acta Crystallographica. Section D, Biological Crystallography, vol. 55, no. 0, pp. 691-693

Keywords 

phytaseBacillusisolation and purificationprotein conformationX ray crystallography6-Phytasecrystallography, X-rayBacillus amyloliquefaciens

Abstract 

A novel bacterial phytase from a Bacillus amyloliquefaciens strain was crystallized using the hanging-drop vapour-diffusion method. The amino-acid sequence of the enzyme does not show any homology to those of other known phytases or phosphatases, with the exception of a phytase from Bacillus subtilis. The enzyme exhibits a thermal stability which is strongly dependent on calcium ions. High-quality single crystals of the enzyme in the absence of calcium ions were obtained using a precipitant solution containing 20% 2-methyl-2,4-pentanediol and 0.1 MMES (pH 6.5). Native diffraction data to 2.0 ? resolution were obtained from a flash-frozen crystal at 110 K using a rotating-anode X-ray source. The crystals belong to space group P212121 with unit-cell dimensions a = 50.4, b = 64.1, c = 104.2 ? and contain one monomer per asymmetric unit. Structure determination using heavy-atom derivative crystals is in progress, along with an effort to crystallize the calcium ion bound form of the enzyme.

Citation 

Acta Crystallographica. Section D, Biological Crystallography, 55(0): 691-693

ISSN 

0907-4449

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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