Crystallization and preliminary crystallographic analysis of laminarinase from Rhodothermus marinus: a case of pseudomerohedral twinning.
Protein Pept Lett
; 15(10): 1142-4, 2008.
Article
em En
| MEDLINE
| ID: mdl-19075828
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 1.95A 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%.
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Base de dados:
MEDLINE
Assunto principal:
Rhodothermus
/
Endo-1,3(4)-beta-Glucanase
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article