Journal:Acta Cryst D:S2059798322002157
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | β<StructureSection load='' size='450' side='right' scene='90/905553/Cv/2' caption=''> | |
===The X-ray crystallography phase problem solved thanks to AlphaFold and RoseTTAFold models: a case study report=== | ===The X-ray crystallography phase problem solved thanks to AlphaFold and RoseTTAFold models: a case study report=== | ||
<big>Irène Barbarin-Bocahu, Marc Graille</big> <ref>doi: 10.1107/S2059798322002157</ref> | <big>Irène Barbarin-Bocahu, Marc Graille</big> <ref>doi: 10.1107/S2059798322002157</ref> | ||
| Line 7: | Line 7: | ||
Here, we take advantage of these high quality models to solve the crystal structure of a yeast protein involved in an mRNA quality control pathway. This article illustrates one of the important applications of 3D protein structure models generated by AlphaFold or RoseTTAFold programs, i.e. in solving the X-ray crystallography phase problem. We discuss the different strategies to generate search models. Finally, this article also contributes to the validation of the very high quality of these models. | Here, we take advantage of these high quality models to solve the crystal structure of a yeast protein involved in an mRNA quality control pathway. This article illustrates one of the important applications of 3D protein structure models generated by AlphaFold or RoseTTAFold programs, i.e. in solving the X-ray crystallography phase problem. We discuss the different strategies to generate search models. Finally, this article also contributes to the validation of the very high quality of these models. | ||
| - | <scene name='90/905553/Cv/ | + | The ''Kl''Nmd4 protein is made of a three layered 𝛼/β/𝛼 core consisting in a central five stranded parallel β-sheet surrounded by six 𝛼-helices (𝛼1 to 𝛼4, 𝛼10 and 𝛼11) on one side and five (𝛼5 to 𝛼9) on the other side. <scene name='90/905553/Cv/4'>Ribbon representation of the KlNmd4 crystal structure</scene> colored from its N-terminal (blue) to its C-terminal (red) extremities. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 13:59, 27 February 2022
β
| |||||||||||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
