Acta Crystallographica Section F
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Acta Crystallographica Section F: Structural Biology Communications is a rapid all-electronic journal, which provides a home for short communications on the crystallization and structure of biological macromolecules. Structures determined through structural genomics initiatives or from iterative studies such as those used in the pharmaceutical industry are particularly welcomed. Articles are available online when ready, making publication as fast as possible, and include unlimited free colour illustrations, movies and other enhancements. The editorial process is completely electronic with respect to deposition, submission, refereeing and publication.enCopyright (c) 2024 International Union of Crystallography2024-03-01International Union of CrystallographyInternational Union of Crystallographyhttp://journals.iucr.orgurn:issn:2053-230XActa Crystallographica Section F: Structural Biology Communications is a rapid all-electronic journal, which provides a home for short communications on the crystallization and structure of biological macromolecules. Structures determined through structural genomics initiatives or from iterative studies such as those used in the pharmaceutical industry are particularly welcomed. Articles are available online when ready, making publication as fast as possible, and include unlimited free colour illustrations, movies and other enhancements. The editorial process is completely electronic with respect to deposition, submission, refereeing and publication.text/htmlActa Crystallographica Section F: Structural Biology Communications, Volume 80, Part 3, 2024textweekly12002-01-01T00:00+00:003802024-03-01Copyright (c) 2024 International Union of CrystallographyActa Crystallographica Section F: Structural Biology Communications52urn:issn:2053-230Xmed@iucr.orgMarch 20242024-03-01Acta Crystallographica Section Fhttp://journals.iucr.org/logos/rss10f.gif
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Still imageThe unbearable burden of peer review?
http://scripts.iucr.org/cgi-bin/paper?me6270
Copyright (c) 2024 International Union of Crystallographyurn:issn:2053-230Xvan Raaij, M.J.2024-03-01doi:10.1107/S2053230X24002024International Union of CrystallographyThe current situation of scientific manuscript peer review is discussed, both generally and as applied to Acta Crystallographica F – Biological Research Communications.ENpeer reviewtext/htmlThe unbearable burden of peer review?text3802024-03-01Copyright (c) 2024 International Union of CrystallographyActa Crystallographica Section Feditorial5252Structure of the GDP-bound state of the SRP GTPase FlhF
http://scripts.iucr.org/cgi-bin/paper?nd5006
The GTPase FlhF, a signal recognition particle (SRP)-type enzyme, is pivotal for spatial–numerical control and bacterial flagella assembly across diverse species, including pathogens. This study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å. The structure exhibits the classical N- and G-domain fold, consistent with related SRP GTPases such as Ffh and FtsY. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis. These topological reconfigurations are similarly evident in Ffh and FtsY, and play a pivotal role in regulating the functions of these hydrolases.Copyright (c) 2024 International Union of Crystallographyurn:issn:2053-230XDornes, A.Mais, C.-N.Bange, G.2024-02-20doi:10.1107/S2053230X24000979International Union of CrystallographyThis study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å, exhibiting the classical N- and G-domain fold. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis.ENflagellar assemblySRP GTPasesGTPasesFlhFnucleotidesThe GTPase FlhF, a signal recognition particle (SRP)-type enzyme, is pivotal for spatial–numerical control and bacterial flagella assembly across diverse species, including pathogens. This study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å. The structure exhibits the classical N- and G-domain fold, consistent with related SRP GTPases such as Ffh and FtsY. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis. These topological reconfigurations are similarly evident in Ffh and FtsY, and play a pivotal role in regulating the functions of these hydrolases.text/htmlStructure of the GDP-bound state of the SRP GTPase FlhFtext3802024-02-20Copyright (c) 2024 International Union of CrystallographyActa Crystallographica Section Fresearch communications5358Expression, purification and crystallization of the photosensory module of phytochrome B (phyB) from Sorghum bicolor
http://scripts.iucr.org/cgi-bin/paper?nj5324
Sorghum, a short-day tropical plant, has been adapted for temperate grain production, in particular through the selection of variants at the MATURITY loci (Ma1–Ma6) that reduce photoperiod sensitivity. Ma3 encodes phytochrome B (phyB), a red/far-red photochromic biliprotein photoreceptor. The multi-domain gene product, comprising 1178 amino acids, autocatalytically binds the phytochromobilin chromophore to form the photoactive holophytochrome (Sb.phyB). This study describes the development of an efficient heterologous overproduction system which allows the production of large quantities of various holoprotein constructs, along with purification and crystallization procedures. Crystals of the Pr (red-light-absorbing) forms of NPGP, PGP and PG (residues 1–655, 114–655 and 114–458, respectively), each C-terminally tagged with His6, were successfully produced. While NPGP crystals did not diffract, those of PGP and PG diffracted to 6 and 2.1 Å resolution, respectively. Moving the tag to the N-terminus and replacing phytochromobilin with phycocyanobilin as the ligand produced PG crystals that diffracted to 1.8 Å resolution. These results demonstrate that the diffraction quality of challenging protein crystals can be improved by removing flexible regions, shifting fusion tags and altering small-molecule ligands.Copyright (c) 2024 International Union of Crystallographyurn:issn:2053-230XShenkutie, S.M.Nagano, S.Hughes, J.2024-02-20doi:10.1107/S2053230X24000827International Union of CrystallographyA heterologous holophytochrome overproduction system has been developed to produce large quantities of three holoprotein constructs of phytochrome B from S. bicolor for crystallization. The results showed that the diffraction quality of the crystals could be improved by removing flexible regions, shifting the fusion tag and changing the type of ligand.ENSorghum bicolorphytochrome Bmaturitycrystallizationdiffraction qualitySorghum, a short-day tropical plant, has been adapted for temperate grain production, in particular through the selection of variants at the MATURITY loci (Ma1–Ma6) that reduce photoperiod sensitivity. Ma3 encodes phytochrome B (phyB), a red/far-red photochromic biliprotein photoreceptor. The multi-domain gene product, comprising 1178 amino acids, autocatalytically binds the phytochromobilin chromophore to form the photoactive holophytochrome (Sb.phyB). This study describes the development of an efficient heterologous overproduction system which allows the production of large quantities of various holoprotein constructs, along with purification and crystallization procedures. Crystals of the Pr (red-light-absorbing) forms of NPGP, PGP and PG (residues 1–655, 114–655 and 114–458, respectively), each C-terminally tagged with His6, were successfully produced. While NPGP crystals did not diffract, those of PGP and PG diffracted to 6 and 2.1 Å resolution, respectively. Moving the tag to the N-terminus and replacing phytochromobilin with phycocyanobilin as the ligand produced PG crystals that diffracted to 1.8 Å resolution. These results demonstrate that the diffraction quality of challenging protein crystals can be improved by removing flexible regions, shifting fusion tags and altering small-molecule ligands.text/htmlExpression, purification and crystallization of the photosensory module of phytochrome B (phyB) from Sorghum bicolortext3802024-02-20Copyright (c) 2024 International Union of CrystallographyActa Crystallographica Section Fresearch communications5966Crystallization and biochemical studies of the NYN domain of human KHNYN
http://scripts.iucr.org/cgi-bin/paper?ek5037
KHNYN is composed of an N-terminal KH-like RNA-binding domain and a C-terminal PIN/NYN endoribonuclease domain. It forms a complex with zinc-finger antiviral protein (ZAP), leading to the degradation of viral or cellular RNAs depending on the ZAP isoform. Here, the production, crystallization and biochemical analysis of the NYN domain (residues 477–636) of human KHNYN are presented. The NYN domain was crystallized with a heptameric single-stranded RNA from the AU-rich elements of the 3′-UTR of interferon lambda 3. The crystal belonged to space group P4132, with unit-cell parameters a = b = c = 111.3 Å, and diffacted to 1.72 Å resolution. The RNase activity of the NYN domain was demonstrated using different single-stranded RNAs, together with the binding between the NYN domain of KHNYN and the zinc-finger domain of ZAP.Copyright (c) 2024 International Union of Crystallographyurn:issn:2053-230XHong, S.Choe, J.2024-02-20doi:10.1107/S2053230X24000943International Union of CrystallographyThe NYN domain of human KHNYN was crystallized with a single-stranded RNA and the crystal diffracted to 1.72 Å resolution. The RNase activity of the NYN domain was also demonstrated using different RNAs, together with the binding between the NYN domain of KHNYN and the zinc-finger domain of ZAP.ENKHNYNZAPRNasesantiviralsKHNYN is composed of an N-terminal KH-like RNA-binding domain and a C-terminal PIN/NYN endoribonuclease domain. It forms a complex with zinc-finger antiviral protein (ZAP), leading to the degradation of viral or cellular RNAs depending on the ZAP isoform. Here, the production, crystallization and biochemical analysis of the NYN domain (residues 477–636) of human KHNYN are presented. The NYN domain was crystallized with a heptameric single-stranded RNA from the AU-rich elements of the 3′-UTR of interferon lambda 3. The crystal belonged to space group P4132, with unit-cell parameters a = b = c = 111.3 Å, and diffacted to 1.72 Å resolution. The RNase activity of the NYN domain was demonstrated using different single-stranded RNAs, together with the binding between the NYN domain of KHNYN and the zinc-finger domain of ZAP.text/htmlCrystallization and biochemical studies of the NYN domain of human KHNYNtext3802024-02-20Copyright (c) 2024 International Union of CrystallographyActa Crystallographica Section Fresearch communications6772