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Purification, crystallization, and preliminary X-ray diffraction studies of tRNA-guanine transglycosylase fromZymomonas mobilis

✍ Scribed by Romier, Christophe; Ficner, Ralf; Reuter, Klaus; Suck, Dietrich

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 399 KB
Volume: 24
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199604)24:4<516::aid-prot11>3.0.co;2-o

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✦ Synopsis

The tRNA modifying enzyme tRNA-guanine transglycosylase (Tgt) catalyzes the exchange of guanine in the first position of the anticodon with the queuine precursor 7-aminomethyl-7-deazaguanine. Tgt from Zymomo-na8 mobilis has been purified by crystallization and further recrystallized to obtain single crystals suitable for X-ray diffraction studies. Crystals were grown by vapor diffusionlgel crystallization methods using PEG 8,000 as precipitant. Macroseeding techniques were employed to produce large single crystals. The crystals of Tgt belong to the monoclinic space group C2 with cell constants a = 92.1 A, b = 65.1 A, c = 71.9 A, and p = 97.5", and contain one molecule per asymmetric unit. A complete diffraction data set from one native crystal has been obtained at 1.85 A resolution. o 19% Wiley-Liss, Inc.

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