التفاصيل البيبلوغرافية
| العنوان: |
Expression, purification, crystallization and preliminary X-ray analysis of eCGP123, an extremely stable monomeric green fluorescent protein with reversible photoswitching properties. |
| المؤلفون: |
Don Paul, Craig, Traore, Daouda A. K., Byres, Emma, Rossjohn, Jamie, Devenish, Rodney J., Kiss, Csaba, Bradbury, Andrew, Wilce, Matthew C. J., Prescott, Mark |
| المصدر: |
Acta Crystallographica: Section F (Wiley-Blackwell); Oct2011, Vol. 67 Issue 10, p1266-1268, 3p |
| مصطلحات موضوعية: |
CRYSTALLIZATION, X-ray crystallography, MONOMERS, BIOLUMINESCENCE assay, JELLYFISHES |
| مستخلص: |
Enhanced consensus green protein variant 123 (eCGP123) is an extremely thermostable green fluorescent protein (GFP) that exhibits useful negative reversible photoswitching properties. eCGP123 was derived by the application of both a consensus engineering approach and a recursive evolutionary process. Diffraction-quality crystals of recombinant eCGP123 were obtained by the hanging-drop vapour-diffusion method using PEG 3350 as the precipitant. The eCGP123 crystal diffracted X-rays to 2.10 Å resolution. The data were indexed in space group P1, with unit-cell parameters a = 74.63, b = 75.38, c = 84.51 Å, α = 90.96, β = 89.92, γ = 104.03°. The Matthews coefficient ( VM = 2.26 Å3 Da−1) and a solvent content of 46% indicated that the asymmetric unit contained eight eCGP123 molecules. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
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