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

L. S. Reshetnikova; C. O.A. Reiser; N. K. Schirmer; H. Berchtold; R. Storm; R. Hilgenfeld; M. Sprinzl

doi:10.1016/0022-2836(91)80058-3

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

L. S. Reshetnikova^*, C. O.A. Reiser, N. K. Schirmer, H. Berchtold, R. Storm, R. Hilgenfeld, M. Sprinzl

^*Corresponding author for this work

Institute of Biochemistry

Universität Bayreuth

8 Citations (Scopus)

Abstract

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.

Original language	English
Journal	Journal of Molecular Biology
Volume	221
Issue number	2
Pages (from-to)	375-377
Number of pages	3
ISSN	0022-2836
DOIs	https://doi.org/10.1016/0022-2836(91)80058-3
Publication status	Published - 20.09.1991

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Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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10.1016/0022-2836(91)80058-3

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title = "Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to high resolution",

abstract = "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 {\AA} 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.",

author = "Reshetnikova, \{L. S.\} and Reiser, \{C. O.A.\} and Schirmer, \{N. K.\} and H. Berchtold and R. Storm and R. Hilgenfeld and M. Sprinzl",

year = "1991",

month = sep,

day = "20",

doi = "10.1016/0022-2836(91)80058-3",

language = "English",

volume = "221",

pages = "375--377",

journal = "Journal of Molecular Biology",

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T1 - Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to high resolution

AU - Reshetnikova, L. S.

AU - Reiser, C. O.A.

AU - Schirmer, N. K.

AU - Berchtold, H.

AU - Storm, R.

AU - Hilgenfeld, R.

AU - Sprinzl, M.

PY - 1991/9/20

Y1 - 1991/9/20

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0025900654

U2 - 10.1016/0022-2836(91)80058-3

DO - 10.1016/0022-2836(91)80058-3

M3 - Journal articles

C2 - 1920424

AN - SCOPUS:0025900654

SN - 0022-2836

VL - 221

SP - 375

EP - 377

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 2

ER -

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

Abstract

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