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Authors
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D.Christendat,
A.Yee,
A.Dharamsi,
Y.Kluger,
A.Savchenko,
J.R.Cort,
V.Booth,
C.D.Mackereth,
V.Saridakis,
I.Ekiel,
G.Kozlov,
K.L.Maxwell,
N.Wu,
L.P.McIntosh,
K.Gehring,
M.A.Kennedy,
A.R.Davidson,
E.F.Pai,
M.Gerstein,
A.M.Edwards,
C.H.Arrowsmith.
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A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were
cloned, expressed and purified for structural studies. Of these, approximately
20% were found to be suitable candidates for X-ray crystallographic or NMR
spectroscopic analysis without further optimization of conditions, providing an
estimate of the number of the most accessible structural targets in the
proteome. A retrospective analysis of the experimental behavior of these
proteins suggested some simple relations between sequence and solubility,
implying that data bases of protein properties will be useful in optimizing high
throughput strategies. Of the first 10 structures determined, several provided
clues to biochemical functions that were not detectable from sequence analysis,
and in many cases these putative functions could be readily confirmed by
biochemical methods. This demonstrates that structural proteomics is feasible
and can play a central role in functional genomics.
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