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Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):30-42.

Methods used in the structure determination of bovine mitochondrial F1 ATPase.

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MRC Laboratory of Molecular Biology, Cambridge, England.


With a size of 372 kDa, the F(1) ATPase particle is the largest asymmetric structure solved to date. Isomorphous differences arising from reacting the crystals with methyl-mercury nitrate at two concentrations allowed the structure determination. Careful data collection and data processing were essential in this process as well as a new form of electron-density modification, 'solvent flipping'. The most important feature of this new procedure is that the electron density in the solvent region is inverted rather than set to a constant value, as in conventional solvent flattening. All non-standard techniques and variations on new techniques which were employed in the structure determination are described.


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