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

Author(s)

Golubev, Alexander M. ^{[1, 2]} ; Rojas, Adriana L. ^[1] ; Nascimento, Alessandro S. ^[1] ; Bleicher, Lucas ^[1] ; Kulminskaya, Anna A. ^[2] ; Eneyskaya, Elena V. ^[2] ; Polikarpov, Igor ^[1]

Affiliation

^[1] Univ Sao Paulo, Inst Fis Sao Carlos, BR-13560970 Sao Carlos, SP - Brazil

^[2] Petersburg Nucl Phys Inst, St Petersburg 188300 - Russia

• Document type: Journal article
• Source: PROTEIN AND PEPTIDE LETTERS; v. 15, n. 10, p. 1142-1144, OCT 2008.
• Web of Science Citations: 1

Abstract

Thermophilic endo-1,3(4)-beta-glucanase (laminarinase) from Rhodothermus marinus was crystallized by the hanging-drop vapor diffusion method. The needle-like crystals belong to space group P2(1) and contain two protein molecules in the asymmetric unit with a solvent content of 51.75%. Diffraction data were collected to a resolution of 1.95 angstrom and resulted in a dataset with an overall R-merge 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%. (AU)

• FAPESP's process: 06/00182-8 - Structural biophysics of nuclear receptors and related proteins
• Grantee: Igor Polikarpov
• Support Opportunities: Research Projects - Thematic Grants