X-ray diffraction studies of the structural state of crossbridges in skinned frog sartorius muscle at low ionic strength

1987 ◽  
Vol 8 (1) ◽  
pp. 39-54 ◽  
Author(s):  
Sengen Xu ◽  
M. Kress ◽  
H. E. Huxley
Keyword(s):  
Ionic Strength ◽  
Structural State ◽  
Sartorius Muscle ◽  
X Ray Diffraction ◽  
X Ray ◽  
Frog Sartorius Muscle ◽  
Low Ionic Strength ◽  
Frog Sartorius

Two-dimensional time-resolved X-ray diffraction studies of live isometrically contracting frog sartorius muscle

1993 ◽  
Vol 14 (3) ◽  
pp. 311-324 ◽  
Author(s):  
J. Bordas ◽  
G. P. Diakun ◽  
F. G. Diaz ◽  
J. E. Harries ◽  
R. A. Lewis ◽  
...  
Keyword(s):  
Sartorius Muscle ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray ◽  
Frog Sartorius Muscle ◽  
Frog Sartorius

Equatorial X-ray intensities and isometric force levels in frog sartorius muscle

1979 ◽  
Vol 132 (1) ◽  
pp. 53-67 ◽  
Author(s):  
Leepo C. Yu ◽  
Jacqueline E. Hartt ◽  
Richard J. Podolsky
Keyword(s):  
Isometric Force ◽  
Sartorius Muscle ◽  
X Ray ◽  
Frog Sartorius Muscle ◽  
Frog Sartorius

RNA polymerase: Preparation and structural analysis of helical polymers

1984 ◽  
Vol 42 ◽  
pp. 152-153
Author(s):  
E. Loren Buhle ◽  
Pamela Rew ◽  
Ueli Aebi
Keyword(s):  
Structural Analysis ◽  
Rna Polymerase ◽  
Molecular Level ◽  
X Ray Diffraction ◽  
Helical Polymers ◽  
X Ray ◽  
E Coli ◽  
The Past ◽  
Ordered Arrays ◽  
Low Ionic Strength

While DNA-dependent RNA polymerase represents one of the key enzymes involved in transcription and ultimately in gene expression in procaryotic and eucaryotic cells, little progress has been made towards elucidation of its 3-D structure at the molecular level over the past few years. This is mainly because to date no 3-D crystals suitable for X-ray diffraction analysis have been obtained with this rather large (MW ~500 kd) multi-subunit (α2ββ'ζ). As an alternative, we have been trying to form ordered arrays of RNA polymerase from E. coli suitable for structural analysis in the electron microscope combined with image processing. Here we report about helical polymers induced from holoenzyme (α2ββ'ζ) at low ionic strength with 5-7 mM MnCl2 (see Fig. 1a). The presence of the ζ-subunit (MW 86 kd) is required to form these polymers, since the core enzyme (α2ββ') does fail to assemble into such structures under these conditions.

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