guidelines for biological crystal structures
Standard experimental tables for biological crystal structures
Each article reporting a biological crystal structure will normally
include standard experimental tables as shown below. Templates and
tools for producing these tables can be found in our Word template at
https://journals.iucr.org/services/wordstyle.html.
Helpful notes and/or examples are given in the second column.
If the macromolecule production and crystallization information are
given in a previous publication then this should be cited. In such cases, Tables 1 and 2 do not need to be included in your article.
|
Source organism
|
|
|
DNA source
|
|
|
Expression vector
|
|
|
Plasmid construction method
|
e.g.
gene synthesis, restriction-ligation, Gibson assembly, Golden Gate assembly
|
|
Forward primer (if restriction-ligation)
|
In the primers, indicate any restriction sites, cleavage sites or introduction of additional residues, e.g. His6 tag
|
|
Reverse primer (if restriction-ligation)
|
|
|
Expression host
|
|
|
Expression details
|
e.g. kifunensine included; SeMet instead of Met; autoinduction media etc.
|
|
Complete amino-acid sequence of the protein produced
|
|
|
|
Method
|
|
|
Plate type
|
|
|
Temperature (°C)
|
|
|
Protein concentration
|
|
|
Buffer composition of protein solution
|
|
|
Composition of reservoir solution
|
|
|
Volume and ratio of drop
|
|
|
Volume of reservoir
|
|
|
Composition of the cryoprotectant
|
|
|
Drop setting
|
Specify if manual, or give the name of the robot
|
|
Seeding
|
yes/no
|
|
|
Diffraction source
|
|
|
Wavelength (Å)
|
|
|
Temperature (K)
|
|
|
Detector
|
|
|
Crystal to detector distance (mm)
|
|
|
Total rotation range (°)
|
|
|
Exposure time per degree (s) or rotation per
image (°)
|
Only include one of these
|
|
Exposure time per image (s)
|
|
|
Space group
|
|
|
a, b, c (Å)
|
|
|
α β, γ (°)
|
|
|
Mosaicity (°)
|
|
|
Resolution range (Å)
|
Indicate any post-processing of data, including anisotropy correction, including resolution limits and completeness in all dimensions
|
|
Total no. of reflections
|
|
|
No. of unique reflections
|
|
|
Completeness (%)
|
|
|
Redundancy
|
|
|
<I/σ(I)>
from merged data
|
|
|
CC1/2
|
|
|
Rr.i.m.
or Rmeas
|
|
|
Overall B factor from Wilson plot (Å2)
|
|
|
|
Resolution range (Å)
|
|
|
Completeness (%)
|
|
|
No. of reflections, working set
|
|
|
No. of reflections, test set
|
|
|
Final Rcryst
|
|
|
Final Rfree
|
|
|
No. of non-H atoms
|
|
|
Protein/nucleic acid
|
|
|
Ions
|
|
|
Ligands
|
|
|
Waters
|
|
|
Total
|
|
|
R.m.s. deviations from ideality
|
Cite the source of restraints/definitions
|
|
Bonds (Å)
|
|
|
Angles (°)
|
|
|
Average B factors (Å2)
|
|
|
Protein/nucleic acid
|
|
|
Ions
|
|
|
Ligands
|
|
|
Waters
|
|
|
Ramachandran plot
|
Cite the source of restraints/definitions
|
|
Favoured regions (%)
|
|
|
Outliers (%)
|
|
|
Unmodelled/incomplete residues (%)
|
|
|
menu
