Protein & Peptide Letters

Author(s): Alexander M. Golubev, Adriana L. Rojas, Alessandro S. Nascimento, Lucas Bleicher, Anna A. Kulminskaya, Elena V. Eneyskaya and Igor Polikarpov

DOI: 10.2174/092986608786071139

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Crystallization and Preliminary Crystallographic Analysis of Laminarinase from Rhodothermus marinus: A Case of Pseudomerohedral Twinning

Page: [1142 - 1144] Pages: 3

  • * (Excluding Mailing and Handling)

Abstract

Thermophilic endo-1,3(4)-β-glucanase (laminarinase) from Rhodothermus marinus was crystallized by the hanging-drop vapor diffusion method. The needle-like crystals belong to space group P21 and contain two protein molecules in the asymmetric unit with a solvent content of 51.75 %. Diffraction data were collected to a resolution of 1.95Å and resulted in a dataset with an overall Rmerge of 10.4% and a completeness of 97.8%. Analysis of the structure factors revealed pseudomerohedral twinning of the crystals with a twin fraction of approximately 42%.

Keywords: Laminarinase, Rhodothermus marinus, crystallization, pseudomerohedral twinning