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Crystal polymorphism in fragment-based lead discovery of ligands of the catalytic domain of UGGT, the glycoprotein folding quality control checkpoint

Abstract:

None of the current data processing pipelines for X-ray crystallography fragment-based lead discovery (FBLD) consults all the information available when deciding on the lattice and symmetry (i.e., the polymorph) of each soaked crystal. Often, X-ray crystallography FBLD pipelines either choose the polymorph based on cell volume and point-group symmetry of the X-ray diffraction data or leave polymorph attribution to manual intervention on the part of the user. Thus, when the FBLD crystals belon...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.3389/fmolb.2022.960248

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Publisher:
Frontiers Media
Journal:
Frontiers in Molecular Biosciences More from this journal
Volume:
9
Article number:
960248
Publication date:
2022-12-14
Acceptance date:
2022-11-11
DOI:
EISSN:
2296-889X
Language:
English
Keywords:
Pubs id:
1315042
Local pid:
pubs:1315042
Deposit date:
2022-12-14

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