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
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