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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.
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Metadata
- Authors
- Abrahams, J. P., & Leslie, A. G. W.
- Venue
- Acta Crystallographica Section D Biological Crystallography
- Published
- 1996-01-01
- Volume
- 52
- Issue
- 1
- Pages
- 30-42
- ISSN
- 0907-4449 (ISSN-L)
- OpenAlex
- W2101446086
- Cited by
- 1,089
- References
- 0
- FWCI
- 51.01
- Type
- journal article
- Language
- en
- Open access
- closed
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- Abrahams, J. P., & Leslie, A. G. W. (1996). Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallographica Section D Biological Crystallography. https://doi.org/10.1107/s0907444995008754
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