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Title
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The quaternary arrangement of HslU and HslV in a cocrystal: a response to Wang, Yale.
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Authors
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M.Bochtler,
H.K.Song,
C.Hartmann,
R.Ramachandran,
R.Huber.
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Ref.
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J Struct Biol, 2001,
135,
281-293.
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PubMed id
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Abstract
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Protease HslV and ATPase HslU form an ATP-dependent protease in bacteria. We
have previously determined the structure of the components of this protease. In
the case of HslU, the structure was derived from HslU-HslV cocrystals, combining
phase information from MAD and the previously determined HslV model. Whereas the
structures of the components were confirmed in detail by later structures, the
quaternary arrangement of HslV and HslU was not reproduced in later crystal
forms. In a recent communication to this journal, Wang attempted a
reinterpretation of our original data to account for this difference. In
response, we demonstrate that difference Pattersons, difference Fouriers,
molecular replacement calculations, R factors, and omit maps all support our
original analysis and prove that the suggested reinterpretation is false by
these criteria. In particular, we show that our crystals are essentially
untwinned and that only the originally reported quaternary arrangement of HslV
and HslU particles is consistent with the experimental data. We finally
demonstrate that Wang's newly introduced R(tpart) method to predict
translational corrections for a subset of the unit cell contents is
systematically flawed.
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