Crystallization Trials Of Globin Domain Of Environmental Stress Protein Rsbr From Saprospira Grandis

Simple item page
dc.contributor.authorBadai, Siti Suriawati
dc.date.accessioned2019-09-11T06:44:53Z
dc.date.available2019-09-11T06:44:53Z
dc.date.issued2011-02
dc.description.abstractRsbR from the coastal scavenger bacterium Saprospira grandis consists of two structural domains, the N-terminal globin domain (residues 12-157) and Cterminal STAS domain (residues 165-276). Observation of the stressosome structure indicates that the globin fold of the N-terminal domain of RsbR might play crucial role as stress sensor in the environmental stress signalling. In this study, we have cloned the gene fragment encoding the globin domain of RsbR and expressed, purified, and crystallized the recombinant protein. Initial crystallization screening of the globin domain of RsbR yielded round shaped crystals. The poor morphology of this crystal was further optimized by screening the pH, analyzing the effect of buffer choice on crystal quality, testing a reasonable range of precipitant concentration, trying different salts from the same chemical class, setting crystallization screens at different temperatures, streak seeding, and screening with the Detergent Screen HT kit. However, no improvement on crystal quality was observed. Four additional recombinant variants of N-RsbR domain were constructed and crystallization trials are currently being performed.en_US
dc.identifier.urihttp://hdl.handle.net/123456789/8858
dc.language.isoenen_US
dc.publisherUniversiti Sains Malaysiaen_US
dc.subjectGlobin Domain Of Environmental Stress Protein Rsbren_US
dc.subjectSaprospira Grandisen_US
dc.titleCrystallization Trials Of Globin Domain Of Environmental Stress Protein Rsbr From Saprospira Grandisen_US
dc.typeThesisen_US
Files
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.71 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Pusat Pengajian Sains Kajihayat - Tesis