Crystallization and preliminary crystallographic analysis of endo-1,3-beta-glucanase from alkaliphilic Nocardiopsis sp. strain F96.

نویسندگان

  • Guntur Fibriansah
  • Sumiko Masuda
  • Raita Hirose
  • Kensaku Hamada
  • Nobuo Tanaka
  • Satoshi Nakamura
  • Takashi Kumasaka
چکیده

Endo-1,3-beta-glucanase, an enzyme that hydrolyzes the 1,3-beta-glycosyl linkages of beta-glucan, belongs to the family 16 glycosyl hydrolases, which are widely distributed among bacteria, fungi and higher plants. Crystals of a family 16 endo-1,3-beta-glucanase from the alkaliphilic Nocardiopsis sp. strain F96 were obtained by the hanging-drop vapour-diffusion method. The crystals belonged to space group P2(1), with unit-cell parameters a = 34.59, b = 71.84, c = 39.67 A, beta = 90.21 degrees, and contained one molecule per asymmetric unit. The Matthews coefficient (VM) and solvent content were 1.8 A3 Da(-1) and 31.8%, respectively. Diffraction data were collected to a resolution of 1.3 A and gave a data set with an overall Rmerge of 6.4% and a completeness of 99.3%.

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عنوان ژورنال:
  • Acta crystallographica. Section F, Structural biology and crystallization communications

دوره 62 Pt 1  شماره 

صفحات  -

تاریخ انتشار 2006