Abstract
With the isomorphous replacement method a preliminary set of protein phases and a first model of the protein structure can be obtained. As we shall see in Chapter 13 such a model can be refined by minimizing the difference between the observed |F|-values and the |F|-values calculated from the model. An easier way to obtain a first model can be followed if the structure of a protein with a homologous amino acid sequence has already been established. The structure of this homologous protein is as it were—borrowed by the protein for which the structure must be determined and serves as a very first model that can subsequently be refined. This procedure is based on the observation that proteins, homologous in their amino acid sequence, have a very similar folding of their polypeptide chain. Also, if for another reason two structures can be expected to be similar, one known and the other unknown, the procedure can be applied.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1999 Springer Science+Business Media New York
About this chapter
Cite this chapter
Drenth, J. (1999). Molecular Replacement. In: Principles of Protein X-ray Crystallography. Springer Advanced Texts in Chemistry. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-3092-0_10
Download citation
DOI: https://doi.org/10.1007/978-1-4757-3092-0_10
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4757-3094-4
Online ISBN: 978-1-4757-3092-0
eBook Packages: Springer Book Archive