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PDBsum entry 2bs7
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References listed in PDB file
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Key reference
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Title
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Impact of natural variation in bacterial f17g adhesins on crystallization behaviour.
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Authors
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L.Buts,
A.Wellens,
I.Van molle,
L.Wyns,
R.Loris,
M.Lahmann,
S.Oscarson,
H.De greve,
J.Bouckaert.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2005,
61,
1149-1159.
[DOI no: ]
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PubMed id
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Abstract
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Since the introduction of structural genomics, the protein has been recognized
as the most important variable in crystallization. Recent strategies to modify a
protein to improve crystal quality have included rationally engineered point
mutations, truncations, deletions and fusions. Five naturally occurring
variants, differing in 1-18 amino acids, of the 177-residue lectin domain of the
F17G fimbrial adhesin were expressed and purified in identical ways. For four
out of the five variants crystals were obtained, mostly in non-isomorphous space
groups, with diffraction limits ranging between 2.4 and 1.1 A resolution. A
comparative analysis of the crystal-packing contacts revealed that the variable
amino acids are often involved in lattice contacts and a single amino-acid
substitution can suffice to radically change crystal packing. A statistical
approach proved reliable to estimate the compatibilities of the variant
sequences with the observed crystal forms. In conclusion, natural variation,
universally present within prokaryotic species, is a valuable genetic resource
that can be favourably employed to enhance the crystallization success rate with
considerably less effort than other strategies.
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Figure 2.
Figure 2 DLS size-distribution diagrams of F17a-G showing (a) a
monodisperse pattern for the second eluted peak from gel
filtration and (b) large aggregates in the first eluted peak. A
similar pattern as in (b) is obtained upon aging of the F17a-G
solution used in (a). The hydrodynamic radius is displayed on
the x axis and each of the ten measurements along the y axis.
The intensities for the distributions are indicated by the
colours blue (absent) to dark red (most prominent).
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Figure 3.
Figure 3 Diffraction patterns of (a) F17a-G in complex with
GlcNAc(  1-)OMe
extending to 1.7 Å resolution, (b) F17b-G in complex with
GlcNAc extending to 2.3 Å resolution and (c) F17e-G in complex
with GlcNAc extending to 2.4 Å resolution.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2005,
61,
1149-1159)
copyright 2005.
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