The Journal of Structural Biology (J. Struct. Biol., JSB) publishes papers dealing with the structural analysis of
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Novel applications of and methodological innovations
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In the context of structural cell biology, papers dealing with cellular architecture and dynamics are particularly welcomed. We see
biomineralization as an important emerging area.
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Crystallization
Notes, Technical Notes and Structure Reports. In addition to regular full-length papers reporting crystal structures and novel methods
and/or mechanisms of crystallization, the Journal of Structural Biology publishes three kinds of short communications - Crystallization
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The primary consideration for eligibility as a Crystallization Note is that the observations
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A Technical Note is similar to a Crystallization Note in format and length and gives a succinct
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Structure Reports concisely document macromolecular
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A Crystallization Note, Technical Note
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For 3D crystals, crystal quality should be demonstrated with a crystal photograph
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Minireviews. JSB will publish minireviews
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Paper of the Year.The Journal of Structural Biology Paper of the Year Award is conferred annually and consists of a cash prize of $1000
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or co-first author of a paper that appeared in JSB in the preceding three years or who had that status (graduate student or fellow) at
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Veselská, R., Janisch, R., 2001. Reaction of the skin fibroblast cytoskeleton to micromanipulation
interventions. J. Struct. Biol. 136, 110–118.
Villiger, W., 1990. Lowicryl resins, in: Hayat, M.A. (Ed.), Colloidal Gold: Principles,
Methods, and Applications. Academic Press, San Diego, Vol. 3, pp. 59–71.
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Table A
Structure Reports
Structure Reports should include the following information
(some of which have example values preceded by a colon) which may be presented in tabular form:
The PDB accession code for the structure.
Source of protein
The source of the original gene sequence and any coding identification.
Whether it is full length or
a fragment(s).
Number of chains and their molecular weights.
If it is a fragment of a gene, how the boundaries were determined,
and its relationship to the entire protein.
The organism in which the protein was expressed and the vector and/or promoter and resistance
markers sufficient to allow another to repeat.
Crystal Space group Unit cell dimensions and angles
Data used in refinement.
Resolution range
high (Å) : 1.75
Resolution range low (Å) : 29.46
Data cutoff (σ(F)) : 0.000
Outlier
cutoff high (RMS(ABS(F))) : Null
Completeness (working+test) (%) : 98.6
Number of reflections : 59490
Fit to data used in refinement
Cross-validation method : Throughout
Free R value test set selection
: Random
R value (working set) : 0.197
Free R value : 0.221
Free R value test set size (%) : 5.100
Free R value test set count : 3007
Estimated error of free R
value : 0.004
Fit in the highest resolution bin
Total number of bins used : 6
Bin resolution range high
(Å) : 1.75
Bin resolution range low (Å) : 1.86
Bin completeness (working+test) (%) : 92.40
Reflections
in bin (working set) : 8758
Bin R value (working set) : 0.3450
Bin free R value
: 0.3750
Bin free R value test set size (%) : 5.10
Bin free R value test set count : 467
Estimated error of bin free R value : 0.017
Number of non-hydrogen atoms used in refinement
Protein atoms
: 4306
Nucleic acid atoms : 0
Heterogen atoms : 132
Solvent atoms : 367
B
values
From Wilson Plot (Å2) : 25.90
Mean B value (overall, Å2)
: 27.30
Rms deviations from ideal values
Bond lengths (Å) : 0.007
Bond angles (°)
: 1.50
Dihedral angles (°) : 24.10
Improper angles (°) : 0.90
Bulk solvent modeling
Method used : Flat Model
KSOL : 0.38
BSOL : 43.37
NCS model : Null
NCS restraints
RMS SIGMA/WEIGHT
Group 1 positional (Å) : Null ; Null
Group 1 B
factor (Å2) : Null ; Null
Temperature (Kelvin) : 100.0
pH
: 8.60
Number of crystals used : 1
Synchrotron (Y/N) : N
Radiation source : Rotating
anode
Beamline : Null
X-ray generator model : Rigaku
Monochromatic or laue (M/L)
: M
Wavelenth or range (Å) : 1.5418
Monochromator : Osmic mirrors
Optics
: Osmic mirrors
Detector type : Image plate
Detector manufacturer : Rigaku Raxis IV
Intensity-integration software : Denzo
Data scaling software : Scalepack
Number of unique reflections :
59657
Resolution range high (Å) : 1.750
Resolution range low (Å) : 29.460
Rejection criteria
(σ(I)) : -3.000
Overall
Completeness for range (%) : 98.6
Data redundancy : Null
Rmerge (I) : Null
Rsym (I) : Null
I/σ(I)
for the data set : Null
In the highest resolution shell
Highest resolution shell, range high (Å) : 1.75
Highest
resolution shell, range low (Å) : 1.81
Completeness for shell (%) : 88.1
Data redundancy in shell : Null
Rmerge for shell (I) : Null
Rsym for shell (I) : Null
I/σ(I)
for shell : Null
Diffraction protocol: Single wavelength
Method used to determine the structure: Molecular replacement
