International Tables for Crystallography (2006). Vol. F. ch. 21.1, pp. 497-506   | 1 | 2 |
https://doi.org/10.1107/97809553602060000707

Chapter 21.1. Validation of protein crystal structures

Chapter index

Accuracy
of unit-cell parameters 21.1.7.1.6
Atomic displacement parameters (temperature factors)
in structure validation 21.1.7.3
Balasubramanian plot 21.1.7.2.2
Bias
model 21.1.4
Chirality 21.1.7.2.1
Chiral volume 21.1.7.2.1
Circular variance plots 21.1.7.2.5
Coordinate errors
estimation of 21.1.7.4.3
Cross validation 21.1.7.4.1
Cα-only model 21.1.7.2.3
Data completeness
and structure validation 21.1.7.1.2
Data redundancy 21.1.7.1.3
Data resolution
and structure validation 21.1.7.1.5
effective 21.1.7.1.5
nominal 21.1.7.1.5
Difference density quality 21.1.7.4.5
Diffraction-component precision index (DPI) 21.1.7.4.3
Directional atomic contact analysis 21.1.7.2.4
DPI (diffraction-component precision index) 21.1.7.4.3
Errors
coordinate, estimation of 21.1.7.4.3
in protein-structure models 21.1.2, 21.1.4, 21.1.5
Frame shift 21.1.2
Free R factor 21.1.3.3, 21.1.7.4.1
G factors 21.1.7.2.7
Hydrogen bonding
analysis of in structure validation 21.1.3.2, 21.1.7.2.4
I/σ(I) ratio 21.1.7.1.4
Luzzati plot 21.1.7.4.3
Merging R factors 21.1.7.1.1
Rmeas 21.1.7.1.1
Rmerge 21.1.7.1.1
Missing symmetry 21.1.7.1.7
Model bias 21.1.4
Model rebuilding 21.1.4
Noncrystallographic symmetry
in structure validation 21.1.7.2.5, 21.1.7.4.4
OOPS 21.1.4
Outliers
in protein-structure models 21.1.3, 21.1.3.1
Overfitting 21.1.3.3
Peptide flip 21.1.3.2, 21.1.7.2.2
Peptides
cis 21.1.7.2.2
trans 21.1.7.2.2
Pooled coefficient of variation 21.1.7.1.1
Pseudosymmetry 21.1.7.1.7
Quality indicators 21.1.3.1, 21.1.7
G factors 21.1.7.2.7
merging R factors 21.1.7.1.1
pooled coefficient of variation 21.1.7.1.1
Ramachandran plot 21.1.3.2, 21.1.7.2.2
multiple-model 21.1.7.2.5
Real-space fit 21.1.3.2, 21.1.7.4.2
Real-space R factor 21.1.7.4.2
Redundancy 21.1.7.1.3
Register error 21.1.2
R factors
crystallographic 21.1.3.3, 21.1.7.4.1
real-space 21.1.7.4.2
Rfree 21.1.3.3, 21.1.7.4.1
Rfree 21.1.3.3, 21.1.7.4.1
Rotamer conformations 21.1.7.2.2
Rotamer side-chain fit 21.1.3.2
SFCHECK 21.1.7.4.2
Side-chain torsion angles 21.1.7.2.2
Signal strength and structure validation 21.1.7.1.4
Solvent
in structure validation 21.1.7.2.6
Space-group assignment 21.1.7.1.7
Structure validation 21.1.1
Balasubramanian plot 21.1.7.2.2
bond angles 21.1.7.2.1
bond lengths 21.1.7.2.1
Cα-only models 21.1.7.2.3
data completeness 21.1.7.1.2
data resolution 21.1.7.1.5
detection of outliers 21.1.3, 21.1.3.1
difference density quality 21.1.7.4.5
directional atomic contact analysis 21.1.7.2.4
geometric parameters 21.1.7.2.1
hydrogen-bonding analysis 21.1.3.2, 21.1.7.2.4
noncrystallographic symmetry 21.1.7.2.5, 21.1.7.4.4
pep-flip value 21.1.3.2
planarity 21.1.7.2.1
quality indicators 21.1.3.1
Ramachandran plot 21.1.3.2, 21.1.7.2.2
real-space fit 21.1.3.2, 21.1.7.4.2
rotamer side-chain fit 21.1.3.2
side-chain torsion angles 21.1.7.2.2
signal strength 21.1.7.1.4
solvent 21.1.7.2.6
stereochemical parameters 21.1.7.2.1
torsion angles 21.1.7.2.2
unit-cell parameters 21.1.7.1.6
Symmetry
missing 21.1.7.1.7
Temperature factors (atomic displacement parameters)
in structure validation 21.1.7.3
Unit-cell parameters
accuracy of 21.1.7.1.6
σA plot 21.1.7.4.3