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PDBsum entry 2erl
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DOI no:
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Acta Crystallogr D Biol Crystallogr
52:469-480
(1996)
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PubMed id:
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A challenging case for protein crystal structure determination: the mating pheromone Er-1 from Euplotes raikovi.
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D.H.Anderson,
M.S.Weiss,
D.Eisenberg.
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ABSTRACT
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Four different phasing methods have been applied to the determination of the
crystal structure of the 40 amino-acid mating pheromone of the unicellular
ciliated protozoan Euplotes raikovi. The difficulties, failures and successes in
attempts to solve the structure by: (1) molecular replacement, (2) direct
phasing using the 'Shake and Bake' algorithm, (3) isomorphous replacement, and
(4) multiple-wavelength anomalous dispersion are described. The structure was
first solved by molecular replacement, and then was the first successful
structure determination by 'Shake and Bake' without the direct involvement of
its authors. A description of the current status of the high-resolution
refinement of the structure is also given. The model is refined against 1 A
resolution data to an R factor of 12.9%, and includes H atoms and discretely
disordered side chains.
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Selected figure(s)
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Figure 4.
Fig. 4. Stereoview of all the
protein atoms in the model
of Er-l, with the anomalous
Fourier superimposed (con-
toured at +3or). There are
peaks only at the locations
of S atoms, showing that
the S atoms are correctly
placed. The view is similar
to that in Fig. l(a) of Weiss
et al.
(1995). This figure was
prepared with the program
FRODO
(Jones, 1978).
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1996,
52,
469-480)
copyright 1996.
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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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T.A.Ramelot,
S.Raman,
A.P.Kuzin,
R.Xiao,
L.C.Ma,
T.B.Acton,
J.F.Hunt,
G.T.Montelione,
D.Baker,
and
M.A.Kennedy
(2009).
Improving NMR protein structure quality by Rosetta refinement: a molecular replacement study.
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Proteins,
75,
147-167.
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PDB codes:
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Y.W.Chen,
E.J.Dodson,
and
G.J.Kleywegt
(2000).
Does NMR mean "not for molecular replacement"? Using NMR-based search models to solve protein crystal structures.
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Structure,
8,
R213-R220.
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G.G.Privé,
D.H.Anderson,
L.Wesson,
D.Cascio,
and
D.Eisenberg
(1999).
Packed protein bilayers in the 0.90 A resolution structure of a designed alpha helical bundle.
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Protein Sci,
8,
1400-1409.
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PDB code:
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I.Usón,
and
G.M.Sheldrick
(1999).
Advances in direct methods for protein crystallography.
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Curr Opin Struct Biol,
9,
643-648.
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W.R.Patterson,
D.H.Anderson,
W.F.DeGrado,
D.Cascio,
and
D.Eisenberg
(1999).
Centrosymmetric bilayers in the 0.75 A resolution structure of a designed alpha-helical peptide, D,L-Alpha-1.
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Protein Sci,
8,
1410-1422.
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PDB code:
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A.M.Deacon,
C.M.Weeks,
R.Miller,
and
S.E.Ealick
(1998).
The Shake-and-Bake structure determination of triclinic lysozyme.
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Proc Natl Acad Sci U S A,
95,
9284-9289.
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H.Hauptman
(1997).
Phasing methods for protein crystallography.
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Curr Opin Struct Biol,
7,
672-680.
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S.E.Ealick
(1997).
Now we're cooking: new successes for shake-and-bake.
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Structure,
5,
469-472.
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Z.Dauter,
V.S.Lamzin,
and
K.S.Wilson
(1997).
The benefits of atomic resolution.
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Curr Opin Struct Biol,
7,
681-688.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
