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Purification, crystallization, and preliminary x-ray diffraction studies of tRNA-guanine transglycosylase from Zymomonas mobilis.
Proteins. 1996 Apr; 24(4):516-9.P

Abstract

The tRNA modifying enzyme tRNA-gnanine transglycosylase (Tgt) catalyzes the exchange of guanine in the first position of the anticodon with the quenine precursor 7-aminomethyl-7-deazagnanine. Tgt from Zymomonas mobilis has been purified by crystallization and further recrystallized to obtain single crystals suitable for X-ray diffraction studies. Crystals were grown by vapor diffusion/gel 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 beta = 97.5 degrees and contain one molecule per asymmetric unit. A complete diffraction data set from one native crystal has been obtained at 1.85 A resolution.

Authors+Show Affiliations

Romier C
European Molecular Biology Laboratory, Structural Biology Programme, Heidelberg, Germany.
Ficner R
No affiliation info available
Reuter K
No affiliation info available
Suck D
No affiliation info available

MeSH

Chromatography, Ion ExchangeCrystallizationMicroscopy, ElectronPentosyltransferasesRecombinant ProteinsX-Ray DiffractionZymomonas

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8860000

Citation

Romier, C, et al. "Purification, Crystallization, and Preliminary X-ray Diffraction Studies of tRNA-guanine Transglycosylase From Zymomonas Mobilis." Proteins, vol. 24, no. 4, 1996, pp. 516-9.
Romier C, Ficner R, Reuter K, et al. Purification, crystallization, and preliminary x-ray diffraction studies of tRNA-guanine transglycosylase from Zymomonas mobilis. Proteins. 1996;24(4):516-9.
Romier, C., Ficner, R., Reuter, K., & Suck, D. (1996). Purification, crystallization, and preliminary x-ray diffraction studies of tRNA-guanine transglycosylase from Zymomonas mobilis. Proteins, 24(4), 516-9.
Romier C, et al. Purification, Crystallization, and Preliminary X-ray Diffraction Studies of tRNA-guanine Transglycosylase From Zymomonas Mobilis. Proteins. 1996;24(4):516-9. PubMed PMID: 8860000.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization, and preliminary x-ray diffraction studies of tRNA-guanine transglycosylase from Zymomonas mobilis. AU - Romier,C, AU - Ficner,R, AU - Reuter,K, AU - Suck,D, PY - 1996/4/1/pubmed PY - 2000/6/20/medline PY - 1996/4/1/entrez SP - 516 EP - 9 JF - Proteins JO - Proteins VL - 24 IS - 4 N2 - The tRNA modifying enzyme tRNA-gnanine transglycosylase (Tgt) catalyzes the exchange of guanine in the first position of the anticodon with the quenine precursor 7-aminomethyl-7-deazagnanine. Tgt from Zymomonas mobilis has been purified by crystallization and further recrystallized to obtain single crystals suitable for X-ray diffraction studies. Crystals were grown by vapor diffusion/gel 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 beta = 97.5 degrees and contain one molecule per asymmetric unit. A complete diffraction data set from one native crystal has been obtained at 1.85 A resolution. SN - 0887-3585 UR - https://www.unboundmedicine.com/medline/citation/8860000/Purification_crystallization_and_preliminary_x_ray_diffraction_studies_of_tRNA_guanine_transglycosylase_from_Zymomonas_mobilis_ L2 - https://doi.org/10.1002/(SICI)1097-0134(199604)24:4<516::AID-PROT11>3.0.CO;2-O DB - PRIME DP - Unbound Medicine ER -