TY - JOUR
T1 - Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to 1.45 Å resolution
AU - Reshetnikova, L. S.
AU - Schirmer, N. K.
AU - Reiser, C. O.A.
AU - Berchtold, H.
AU - Storm, R.
AU - Hilgenfeld, R.
AU - Sprinzl, M.
N1 - Funding Information:
We thank A. LOw for HPLC analysis. This work was supported by the Deutsche Forschungs-gemeinschaft, SFB 213.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1992/8/2
Y1 - 1992/8/2
N2 - Intact elongation factor Tu from Thermus thermophilus HB8 was crystallized in the presence of guanosine-5'-diphosphate (GDP), guanosine-5'-(β,γ-imido)triphosphate (GPPNP), guanosine-5'-(β,γ-methylene)triphosphate (GPPCP), p3-1-(2-nitro)phenylethylguanosine- 5'-triphosphate (caged GTP) and elongation factor Ts. An attempt to crystallize a ternary complex of EF-Tu·GPPNP with Phe-tRNAPhe was made. The crystals of EF-Tu obtained with GPPNP or GPPCP, respectively, were suitable for X-ray diffraction analysis at very high resolution.
AB - Intact elongation factor Tu from Thermus thermophilus HB8 was crystallized in the presence of guanosine-5'-diphosphate (GDP), guanosine-5'-(β,γ-imido)triphosphate (GPPNP), guanosine-5'-(β,γ-methylene)triphosphate (GPPCP), p3-1-(2-nitro)phenylethylguanosine- 5'-triphosphate (caged GTP) and elongation factor Ts. An attempt to crystallize a ternary complex of EF-Tu·GPPNP with Phe-tRNAPhe was made. The crystals of EF-Tu obtained with GPPNP or GPPCP, respectively, were suitable for X-ray diffraction analysis at very high resolution.
UR - http://www.scopus.com/inward/record.url?scp=0027109322&partnerID=8YFLogxK
U2 - 10.1016/0022-0248(92)90270-S
DO - 10.1016/0022-0248(92)90270-S
M3 - Journal articles
AN - SCOPUS:0027109322
SN - 0022-0248
VL - 122
SP - 360
EP - 365
JO - Journal of Crystal Growth
JF - Journal of Crystal Growth
IS - 1-4
ER -
