Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to high resolution

The intact elongation factor Tu from the extreme thermophile Thermus thermophilus has been crystalized as a complex with the GTP analogue guanosine-5′-(β-γ-imido)triphosphate. The crystals are very stable in the X-ray beam and diffract to 1·9 Å resolution. They exhibit space group C2, with a = 150·(...

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Bibliographic Details
Published inJournal of molecular biology Vol. 221; no. 2; pp. 375 - 377
Main Authors Reshetnikova, L.S., Reiser, C.O.A., Schirmer, N.K., Berchtold, H., Storm, R., Hilgenfeld, R., Sprinzl, M.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 20.09.1991
Subjects
Crystallization
Electrophoresis, Polyacrylamide Gel
elongation factor Tu
guanine nucleotide-binding protein
Peptide Elongation Factor Tu - chemistry
Thermus thermophilus
Thermus thermophilus - chemistry
X-ray crystallography
X-Ray Diffraction
Thermus thermophilus
X-ray crystallography
EF
elongation factor Tu
guanine nucleotide-binding protein
GPPNP
crystallization
PAGE
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Summary:The intact elongation factor Tu from the extreme thermophile Thermus thermophilus has been crystalized as a complex with the GTP analogue guanosine-5′-(β-γ-imido)triphosphate. The crystals are very stable in the X-ray beam and diffract to 1·9 Å resolution. They exhibit space group C2, with a = 150·(36) A ̊ , b = 99·6(3) A ̊ , c = 40·1(1) A ̊ , β = 95·4(2)°, and contain one elongation factor Tu molecule per asymmetric unit.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:0022-2836
1089-8638
DOI:10.1016/0022-2836(91)80058-3