TY - JOUR
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.
N1 - Copyright:
Copyright 2015 Elsevier B.V., All rights reserved.
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 - http://www.scopus.com/inward/record.url?scp=0025900654&partnerID=8YFLogxK
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 -
