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Crystallization and preliminary X-ray diffraction analysis of a novel wild-type blue fluorescent protein from Vibrio vulnificus CKM-1.

ABSTRACT: The use of green fluorescent protein (GFP) for non-invasive in vivo imaging is limited to aerobic systems, as chromophore formation requires oxygen. However, a novel NADPH-dependent blue fluorescent protein from Vibrio vulnificus CKM-1 (BFPvv) that emits blue fluorescence in both aerobic and anaerobic systems has recently been discovered. Wild-type BFPvv was overexpressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method. The resulting BFPvv crystals diffracted to a resolution of 1.9 Å and belonged to space group P3, with unit-cell parameters a = b = 96.62, c = 214.511 Å. Assuming the presence of eight molecules in the unit cell, the solvent content was estimated to be ~56.16%.

SUBMITTER: Liu CF

PROVIDER: S-EPMC3325817 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of a novel wild-type blue fluorescent protein from Vibrio vulnificus CKM-1.

Liu Chin-Feng CF Kao Chao-Hung CH Su Yen-Chao YC Chen Yeh Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20120327 Pt 4

The use of green fluorescent protein (GFP) for non-invasive in vivo imaging is limited to aerobic systems, as chromophore formation requires oxygen. However, a novel NADPH-dependent blue fluorescent protein from Vibrio vulnificus CKM-1 (BFPvv) that emits blue fluorescence in both aerobic and anaerobic systems has recently been discovered. Wild-type BFPvv was overexpressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method. The resulting BFPvv crystals d ...[more]

PMID: 22505417

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