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Figure 2.
Fig. 2. Comparison of the water structure around Hm GlcDH
to that surrounding other proteins. (A) The dependence of the
water to protein residue ratio (ordinate) against the resolution
in Å (abscissa) for the structure determinations of all
proteins solved between 3.5- and 0.5-Å resolution. Only
the points in the lower 5% and above 95% are shown. The lower
dashes, crosses, and upper dashes mark the 10, 50, and 90%
boundaries for the data, respectively. The data point,
corresponding to the Hm GlcDH, is shown by a large diamond. (B)
A least squares line drawn through points that represent the B
factors of the water structure normalized by the average B
factor of the protein atoms (ordinate) plotted against the ratio
of the number of water molecules to the number of protein atoms
in a given structure (abscissa). The plot covers the 263
structures determined in the resolution range 1.55–1.65
Å for proteins that are of equivalent or greater size to
Hm GlcDH. Each structure is represented on the plot by a
diamond, except for the GlcDH structure, which is shown as a
square. (C) A comparison of the distribution of the distance of
the water molecules from the protein surface between the Hm
GlcDH structure (black) and that of the average of the subset of
263 structures (hatched) as defined in B. The histogram shows
the number of water molecules per residue that fall into
specific distance bands from the protein surface. The abscissa
is labeled with the midpoint of each range. Waters with partial
occupancy were not included in the analysis.
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