Crystallization and Preliminary Crystallographic Analysis of Laminarinase from Rhodothermus marinus: A Case of Pseudomerohedral Twinning
| Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
|---|---|
| Data(s) |
20/10/2012
20/10/2012
2008
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| Resumo |
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%. Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)[04/08070-9] Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)[06/00182-8] Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Presidium of Russian Academy of Sciences Presidium of Russian Academy of Sciences |
| Identificador |
PROTEIN AND PEPTIDE LETTERS, v.15, n.10, p.1142-1144, 2008 0929-8665 http://producao.usp.br/handle/BDPI/30200 10.2174/092986608786071139 |
| Idioma(s) |
eng |
| Publicador |
BENTHAM SCIENCE PUBL LTD |
| Relação |
Protein and Peptide Letters |
| Direitos |
restrictedAccess Copyright BENTHAM SCIENCE PUBL LTD |
| Palavras-Chave | #Laminarinase #Rhodothermus marinus #crystallization #pseudomerohedral twinning #MONOCLINIC CRYSTAL FORM #PROTEIN CRYSTALLOGRAPHY #DIFFRACTION DATA #Biochemistry & Molecular Biology |
| Tipo |
article original article publishedVersion |
