International Tables for Crystallography (2006). Vol. F. ch. 4.3, pp. 100-110   | 1 | 2 |
https://doi.org/10.1107/97809553602060000662

Chapter 4.3. Application of protein engineering to improve crystal properties

Chapter index

Crystallization
improving protein solubility 4.3.2
promotion of a crystal form 4.3.7
use of fusion proteins 4.3.3
Crystal quality
and protein engineering 4.3.1, 4.3.5
Fusion proteins 4.3.3
Glycosylation 4.3.6
Heavy-atom sites in protein engineering 4.3.8
Mutations
acceleration of crystallization 4.3.4
improving crystal quality 4.3.5
site-directed 4.3.1
surface 4.3.2, 4.3.2
Post-translational modifications 4.3.6
Protein engineering
acceleration of crystallization 4.3.4
creation of heavy-atom sites 4.3.8
fusion proteins 4.3.3
improving crystal quality 4.3.1, 4.3.5
improving protein solubility 4.3.2
promotion of a crystal form 4.3.7
site-directed mutagenesis 4.3.1
surface mutations 4.3.2, 4.3.2
Protein expression
post-translational modifications 4.3.6
Protein heterogeneity 4.3.6
avoidance of 4.3.6
Proteolysis
non-specific 4.3.3
prevention of 4.3.3
proteolytic trimming 4.3.5
Selenomethionine 4.3.8
Shine–Dalgarno sequence 4.3.6
Site-directed mutagenesis 4.3.1
Solubility of proteins, improvement of 4.3.2
Surface mutations 4.3.2, 4.3.2
Telluromethionine 4.3.8