International Tables for Crystallography (2006). Vol. F. ch. 3.1, pp. 65-80   | 1 | 2 |
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
Baculovirus expression systems 3.1.4.3
AcNPV 3.1.4.3
BmNPV 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
E. coli expression systems 3.1.4.1, 3.1.4.1
Expression systems 3.1.3.1, 3.1.4
baculoviruses 3.1.4.3
constitutive 3.1.4.1, 3.1.4.1
constructs 3.1.3, 3.1.3.2
E. coli 3.1.4.1, 3.1.4.1
fermentation 3.1.4.1
growth media 3.1.4.1
inducible 3.1.4.1, 3.1.4.1, 3.1.4.1
insect cell–virus 3.1.4.3
mammalian cells 3.1.4.4
misfolded proteins 3.1.4.1
plasmids 3.1.4.1, 3.1.4.1
post-translational modifications 3.1.2, 3.1.3.1, 3.1.4.2, 3.1.6.1
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
Glycosylation 3.1.2, 3.1.4.2, 3.1.4.3
Hydrophobic interaction chromatography 3.1.5.1
Hydroxyapatite chromatography 3.1.5.1
Hyperglycosylation 3.1.4.2, 3.1.4.2
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
PCR (polymerase chain reaction) 3.1.3.2, 3.1.3.2, 3.1.3.2, 3.1.3.2, 3.1.3.2
Polyethylene glycol (PEG) 3.1.5.1
Polymerase chain reaction (PCR) 3.1.3.2, 3.1.3.2, 3.1.3.2, 3.1.3.2, 3.1.3.2
Post-translational modifications 3.1.2, 3.1.3.1, 3.1.4.2, 3.1.6.1
Precipitants
ammonium sulfate 3.1.5.1
Protein engineering 3.1.1
Protein expression 3.1.1, 3.1.3.1, 3.1.4
baculoviruses 3.1.4.3
constitutive 3.1.4.1, 3.1.4.1
constructs 3.1.3, 3.1.3.2
fermentation 3.1.4.1
growth media 3.1.4.1
inducible 3.1.4.1, 3.1.4.1, 3.1.4.1
in E. coli 3.1.4.1, 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
plasmids 3.1.4.1, 3.1.4.1
post-translational modifications 3.1.2, 3.1.3.1, 3.1.4.2, 3.1.6.1
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
Proteolysis
in E. coli 3.1.4.1
N-end rule 3.1.4.1
of recombinant proteins 3.1.4.1
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
Shine–Dalgarno sequence 3.1.4.1, 3.1.4.1
Size-exclusion chromatography 3.1.5.1
Storage of proteins 3.1.6.2
T7 polymerase expression system 3.1.4.1
Tags 3.1.3.3
removal of 3.1.3.3
Transfection 3.1.4.4
Transfer RNA
low-abundance 3.1.4.1
Yeasts as expression systems 3.1.4.2