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- Title
Purification, crystallization and preliminary X-ray diffraction studies of UDP-glucose:tetrahydrobiopterin α-glucosyltransferase (BGluT) from Synechococcus sp. PCC 7942.
- Authors
Killivalavan, Asaithambi; Zhuang, Ningning; Park, Young Shik; Lee, Kon Ho
- Abstract
A UDP-glucose:tetrahydrobiopterin α-glucosyltransferase (BGluT) enzyme was discovered in the cyanobacterium Synechococcus sp. PCC 7942 which transfers a glucose moiety from UDP-glucose to tetrahydrobiopterin (BH4). BGluT protein was overexpressed with selenomethionine labelling for structure determination by the multi-wavelength anomalous dispersion method. The BGluT protein was purified by nickel-affinity and size-exclusion chromatography. It was then crystallized by the hanging-drop vapour-diffusion method using a well solution consisting of 0.1 M bis-tris pH 5.5, 19%( w/ v) polyethylene glycol 3350 with 4%( w/ v) D(+)-galactose as an additive. X-ray diffraction data were collected to 1.99 Å resolution using a synchrotron-radiation source. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 171.35, b = 77.99, c = 53.77 Å, β = 90.27°.
- Subjects
GLUCOSE; TETRAHYDROBIOPTERIN; GLYCOSYLTRANSFERASES; SYNECHOCOCCUS; X-rays
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2014, Vol 70, Issue 2, p203
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X13034298