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Figure 5.
Figure 5. The two conformations of 92K built into the
2Fo 2 Fc (blue) and Fo 2 Fc (magenta) electron density
maps, contoured at 1s and 3.5s respectively, calculated
from a model that had alanine at position 92. The sub-
sequent refinement of the model with the alternate 92K
conformations showed no electron density for the C
d
and N
z
atoms for conformer 1 or for the N
z
for conformer
2, which is indicative of increased mobility of the 92K
side-chain. The electron density maps displayed might
suggest the native isoleucine at this position. The lysine
mutation was confirmed by DNA sequencing and mass
spectrometry (data not shown). Moreover, none of the
four most frequent isoleucine conformers could be built
into these electron density maps (see Supplementary
Material).
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