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

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.

Table 1
Macromolecule production information

For all recombinant proteins, a complete DNA sequence/plasmid map should be provided as supplementary material.

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

Table 2

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

Table 3
Data collection and processing

Values given in parentheses are for the highest resolution shell.

Diffraction source
Wavelength (Å)
Temperature (K)
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 (%)
<I/σ(I)> from merged data
Rr.i.m. or Rmeas
Overall B factor from Wilson plot (Å2)

Table 4
Structure refinement

Values given in parentheses are for the highest resolution shell.

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
R.m.s. deviations from ideality Cite the source of restraints/definitions
Bonds (Å)
Angles (°)
Average B factors (Å2)
Protein/nucleic acid
Ramachandran plot Cite the source of restraints/definitions
Favoured regions (%)
Outliers (%)
Unmodelled/incomplete residues (%)
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