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Methods used in the structure determination of bovine mitochondrial F-1 ATPase

Date Issued
1996-01-01
Author(s)
Abrahams, J. P.  
Leslie, A. G. W.
DOI
10.1107/s0907444995008754
Abstract
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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