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FEBS Letters
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FEBS Letters
Article . 1991 . Peer-reviewed
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The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution

The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution

Abstract

The structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster has been determined by X‐ray diffraction at 2.5A˚resolution. The insect enzyme crystallizes in space groupP212121 with lattice constantsa=86.60,b=116.80,c=151.58A˚. Molecular replacement with rabbit muscle aldolase as a search model has been employed to solve the structure. To improve the initial phases real space averaging, including phase extension from 4.0 to 2.5A˚, has been applied. Refinement of the atomic positions by molecular dynamics resulted in a crystallographicR‐factor of 0.214. The tertiary structure resembles in most parts that of the vertebrate aldolase from rabbit muscle. Significant differences were found in surface loops and the N‐ and C‐terminal regions of the protein. Here we present the first aldolase structure where the functionally important C‐terminal arm is described completely.

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
95
Top 10%
Top 10%
Top 10%
bronze