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

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

Journal Name: Protein & Peptide Letters

Volume 15 , Issue 10 , 2008

Become EABM
Become Reviewer

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

Rights & PermissionsPrintExport Cite as


Article Details

VOLUME: 15
ISSUE: 10
Year: 2008
Page: [1142 - 1144]
Pages: 3
DOI: 10.2174/092986608786071139
Price: $58

Article Metrics

PDF: 4