Methods used in the structure determination of bovine mitochondrial F1 ATPase

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.