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Title
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Crystals of the trp repressor-operator complex suitable for X-ray diffraction analysis.
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Authors
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A.Joachimiak,
R.Q.Marmorstein,
R.W.Schevitz,
W.Mandecki,
J.L.Fox,
P.B.Sigler.
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Ref.
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J Biol Chem, 1987,
262,
4917-4921.
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PubMed id
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Abstract
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Crystals of a simulated trp repressor-operator complex have been grown that are
large enough and are sufficiently well ordered and durable to provide a high
quality molecular image of this regulatory protein X DNA complex to better than
3-A resolution. The "operator" consists of a 2-fold rotationally symmetric
18-base pair duplex that is extended by a dT residue at both 5'-termini. This
system exhibits extensive crystal polymorphism. The crystal form and diffraction
properties are very sensitive to the length and terminal structure of the
operator fragment, as well as the type and concentration of multivalent ions.
When combined with the experience reported by others, our results do not support
a consistent strategy for crystallization of protein X DNA complexes.
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