International Tables for Crystallography (2006). Vol. F. ch. 3.1, pp. 65-80
https://doi.org/10.1107/97809553602060000659 |
Chapter 3.1. Preparing recombinant proteins for X-ray crystallography
Chapter index
Affinity chromatography 3.1.5.2
Ammonium sulfate 3.1.5.1
Anion-exchange chromatography 3.1.5.1
Autographa californica nuclear polyhedrosis virus (AcNPV) 3.1.4.3
Bombyx mori nuclear polyhedrosis virus (BmNPV) 3.1.4.3
Chaperones
use in protein folding 3.1.4.1
Chromatography 3.1.5.1
affinity 3.1.5.2
anion-exchange 3.1.5.1
dye-ligand 3.1.5.1
hydrophobic interaction 3.1.5.1
hydroxyapatite 3.1.5.1
immuno-affinity 3.1.5.2
size-exclusion 3.1.5.1
Codon usage, effect on expression levels 3.1.4.1
Dye-ligand chromatography 3.1.5.1
baculoviruses 3.1.4.3
fermentation 3.1.4.1
growth media 3.1.4.1
insect cell–virus 3.1.4.3
mammalian cells 3.1.4.4
misfolded proteins 3.1.4.1
preparation of cDNA clones 3.1.3.2
T7 polymerase 3.1.4.1
yeasts 3.1.4.2
Fusion proteins 3.1.3.3
Hydrophobic interaction chromatography 3.1.5.1
Hydroxyapatite chromatography 3.1.5.1
Immuno-affinity chromatography 3.1.5.2
Insect cell–virus expression systems 3.1.4.3
Inteins 3.1.3.3
Isoelectric focusing 3.1.6.1
Low-abundance tRNAs 3.1.4.1
Mammalian-cell expression systems 3.1.4.4
Mammalian-cell inducible promoters 3.1.4.4
Mass spectrometry 3.1.6.1
Misfolded proteins 3.1.4.1
Molecular biology 3.1.1
N-terminal heterogeneity 3.1.6.1
Polyethylene glycol (PEG) 3.1.5.1
Precipitants
ammonium sulfate 3.1.5.1
Protein engineering 3.1.1
baculoviruses 3.1.4.3
fermentation 3.1.4.1
growth media 3.1.4.1
insect cell–virus 3.1.4.3
in yeasts 3.1.4.2
mammalian cells 3.1.4.4
misfolded proteins 3.1.4.1
preparation of cDNA clones 3.1.3.2
T7 polymerase 3.1.4.1
Protein folding 3.1.4.1
in vivo 3.1.4.1
misfolded proteins 3.1.4.1
refolding 3.1.5.3
use of chaperones 3.1.4.1
Protein purification 3.1.5
chromatography 3.1.5.1
isoelectric focusing 3.1.6.1
mass spectrometry 3.1.6.1
N-terminal heterogeneity 3.1.6.1
sample heterogeneity 3.1.6.1
SDS–PAGE 3.1.6.1
Protein refolding 3.1.5.3
Proteins, storage of 3.1.6.2
Recombinant proteins 3.1.1
incorporation of selenomethionine 3.1.3.1
minimizing proteolysis of 3.1.4.1
toxicity of, to host 3.1.4.1
SDS–PAGE 3.1.6.1
Selenomethionine 3.1.3.1
Sequence tags 3.1.3.3
Size-exclusion chromatography 3.1.5.1
Storage of proteins 3.1.6.2
T7 polymerase expression system 3.1.4.1
Transfection 3.1.4.4
Transfer RNA
low-abundance 3.1.4.1
Yeasts as expression systems 3.1.4.2