forthcoming articles in Acta Crystallographica Section F

The following articles are a selection of those recently accepted for publication in Acta Crystallographica Section F: Structural Biology and Crystallization Communications.

This list will generally be short, as papers in this journal are published online as soon as proofs are returned.

See also Forthcoming articles in all IUCr journals.

Accepted 29 March 2015

Expression, purification and crystallization of a family 55 [beta]-1,3-glucanase from Chaetomium thermophilum

A. C. Papageorgiou and D. Li

Synopsis: A [beta]-1,3-glucanase from the thermophilic fungus C. thermophilum was overexpressed in P. pastoris, purified and crystallized. In situ diffraction at synchrotron and seeding were used to obtain reproducible crystals. A complete data set to 2.0 Å resolution was collected using an in-house X-ray generator.

Accepted 25 March 2015

A preliminary X-ray study of YrbI from Burkholderia pseudomallei

J. Park, D. Lee, M. Kim, D. Y. Kim and D. H. Shin

Accepted 24 March 2015

Cloning, expression, purification, crystallization, and X-ray crystallographic analysis of CofB, the minor pilin subunit of CFA/III from human enterotoxigenic Escherichia coli

K. Kawahara, H. Oki, S. Fukakusa, T. Maruno, Y. Kobayashi, D. Motooka, T. Taniguchi, T. Honda, T. Iida, S. Nakamura and T. Ohkubo

Synopsis: The CFA/III minor pilin subunit, CofB, was crystallized. An N-terminal hydrophobic portion of CofB was truncated to enable initial crystallization. Dehydration of preliminary crystals yielded higher resolution diffraction patterns.

Accepted 24 March 2015

Preliminary crystallographic analysis of the AtBAG5 -calmodulin protein complex

B. Cui, S. Fang, Y. Xing, Y. Shen and X. Yang

Accepted 24 March 2015

Crystallographic study of a novel DNA-binding domain of human HLTF involved in the template-switching pathway to avoid the replication arrest caused by DNA damage

Y. Ikegaya, K. Hara, A. Hishiki, H. Yokoyama and H. Hashimoto

Synopsis: Crystallization and diffraction studies of the HIRAN domain of human HLTF

Accepted 21 March 2015

Crystallization and preliminary X-ray diffraction analysis of the two distinct types of zebrafish [beta]2-microglobulin

Z. Chen, N. Zhang, S. Lu, M. Tariq, J. Wang and C. Xia

Synopsis: Diffraction data from crystals of zebrafish (Danio rerio) [beta]2-microglobulins type I and type II (Dare-[beta]2m-I and Dare-[beta]2m-II) were collected to 1.6 Å and 1.9 Å resolutions, respectively. Both crystals belonged to space group P212121, with unit-cell parameters a = 38.2 Å, b = 50.4 Å, c = 50.9 Å for Dare-[beta]2m-I, and a = 38.9, b = 52.7, c = 65.8 Å for Dare-[beta]2m-II. Each asymmetric unit contained one molecule. The Matthews coefficient and solvent content of Dare-[beta]2m-I and Dare-[beta]2m-II were calculated to 2.22 Å3 Da-1 and 45%, and 3.01 Å3 Da-1 and 59%, respectively.

Accepted 20 March 2015

Multiple crystal forms of N,N'-di­acetylchitobiose de­acetylase from Pyrococcus furiosus

T. Nakamura, M. Niiyama, W. Hashimoto, K. Ida, M. Abe, J. Morita and K. Uegaki

Accepted 17 March 2015

Structure of Plasmodium falciparum orotate phosphoribosyl-transferase with autologous inhibitory protein- protein interactions

S. Kumar, K. Krishnamoorthy, D. G. Mudeppa and P. K. Rathod

Synopsis: Plasmodium falciparum orotate phosphoribosyl transferase (PfOPRTase), a potential target of antimalarial drugs and a conduit for prodrugs, crystalized as an 8-molecule per asymmetric unit structure (PDB id: 4fym) including some unique parasite-specific auto-inhibitory interactions between catalytic dimers.

Accepted 15 March 2015

Large-volume protein crystal growth for neutron macromolecular crystallography

J. D. Ng, J. K. Baird, L. Coates, J. M. Garcia-Ruiz, T. A. Hodge and S. Huang

Accepted 12 March 2015

Structure of human dual-specificity phosphatase 7, a potential cancer drug target

G. T. Lountos, B. P. Austin, J. E. Tropea and D. S. Waugh

Synopsis: The crystal structure of the catalytic domain of human dual-specificity phosphatase 7 (C232S) is presented at 1.67 Å resolution.

Accepted 11 March 2015

Three-dimensional structures in the design of therapeutics targeting parasitic protozoa: reflections on past, present and future

W. G. J. Hol

Synopsis: A review and historical perspective covering the many different aspects of antiparasitic drug discovery in particular targeting protists (hereafter called protozoa) is presented. The key role of structural studies in the process is highlighted and specific high-profile examples are given.

Accepted 6 March 2015

Structure of an ADP ribosylation factor ARF1 from Entamoeba histolytica bound to Mg2+-GDP

D. A. Serbzhinskiy, M. C. Clifton, B. Sankaran, B. L. Staker, T. E. Edwards and P. J. Myler

Synopsis: ADP-ribosylation factors (ARFs) are highly conserved proteins present in all Eukarya. The structure of ARF from E. histolytica is described and compared with orthologs from other species.

Accepted 27 February 2015

Iron superoxide dismutases in eukaryotic pathogens: new insights from Apicomplexa and Trypanosoma structures

I. Q. H. Phan, D. R. Davies, N. S. Moretti, D. Shanmugam, I. Cestari, A. Anupama, J. W. Fairman, T. E. Edwards, K. Stuart, S. Schenkman and P. J. Myler

Synopsis: Superoxide dismutases (SODs) catalyze the conversion of superoxide to molecular oxygen, thus protecting organisms against toxic radicals. Iron-dependent SODs from T. cruzi, L. major and B. bovis exist as multiple isoforms with distinct structural features.

Accepted 25 February 2015

Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?

E.-P. Kumpula and I. Kursula

Synopsis: In this review, current structural understanding of the apicomplexan glideosome and actin regulation is described.

Accepted 12 February 2015

Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase

D. A. Robinson and P. G. Wyatt

Synopsis: N-Myristoyltransferase (NMT) has been shown to be an attractive target for the development of novel therapeutic agents for the treatment of human African trypanosomiasis. A fragment library has been screened using NMR spectroscopy and the binding mode of hits was confirmed by X-ray crystallography using L. major NMT as a structural surrogate.

Accepted 9 February 2015

The structure of hookworm platelet inhibitor (HPI), a CAP superfamily member from Ancylostoma caninum

D. Ma, I. M. B. Francischetti, J. M. C. Ribeiro and J. F. Andersen

Synopsis: Hookworm platelet inhibitor belongs to the cysteine-rich/antigen-5/pathogenesis-related-1 (CAP) protein family. It has been linked with integrin-antagonist, antiplatelet activity found in extracts of A. caninum hookworms.

Accepted 5 February 2015

Production, purification and crystallization of a trans-sialidase from Trypanosoma vivax

C. L. F. Haynes, P. Ameloot, H. Remaut, N. Callewaert, Y.G.-J. Sterckx and S. Magez

Synopsis: The production, purification and crystallization of a recently identified trans-sialidase from T. vivax is described. The purified enzyme is active and produces diffraction-quality crystals using the sitting-drop vapour-diffusion method. The crystals belonged to space group P212121 and diffracted to 2.5 Å resolution.

Accepted 4 February 2015

Structure of a histidine triad family protein from Entamoeba histolytica bound to sulfate, AMP and GMP

D. D. Lorimer, R. Choi, A. Abramov, S. Nakazawa-Hewitt, A. S. Gardberg, W. C. Van Voorhis, B. L. Staker, P. J. Myler and T. E. Edwards

Synopsis: Structures of the histidine triad family protein from E. histolytica were solved in complex with sulfate, AMP or GMP. The three structures show very similar nucleotide poses, with the sulfate occupying the same space as the [alpha]-phosphate of the nucleotides.

Accepted 27 January 2015

Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia

J. Abendroth, R. Choi, A. Wall, M. C. Clifton, C. M. Lukacs, B. L. Staker, W. van Voorhis, P. Myler, D. D. Lorimer and T. E. Edwards

Synopsis: Structures of aspartate aminotransferases from eukaryotic pathogens were solved in complex with pyridoxal phosphate. The four structures show either the open or the closed conformation of the enzyme. The structures highlight the challenges for structure-based design of inhibitors targeting the active site, while showing options for inhibitor design targeting the N-terminal arm.

Accepted 16 January 2015

X-ray structure of Plasmodium falciparum di­hydroorotate de­hydrogenase bound to a potent and selective N-phenylbenzamide inhibitor reveals novel binding-site interactions

X. Deng, D. Matthews, P. K. Rathod and M. A. Phillips

Synopsis: The X-ray structure of the antimalarial drug target dihydroorotate dehydrogenase bound to a potent and selective benzamide-based inhibitor shows novel binding-site interactions.

Accepted 15 January 2015

Recombinant production, crystallization and crystal structure determination of di­hydroorotate de­hydrogenase from Leishmania (Viannia) braziliensis

R. Almeida Garcia Reis, E. Lorenzato, V. C. Silva and M. C. Nonato

Synopsis: The crystal structure of L. (V.) braziliensis dihydroorotate dehydrogenase, a potential target for drug development against cutaneous leishmaniasis, is reported.

Accepted 6 January 2015

Structure of Cryptosporidium IMP de­hydrogenase bound to an inhibitor with in vivo antiparasitic activity

Y. Kim, M. Makowska-Grzyska, S. K. Gorla, D. R. Gollapalli, G. D. Cuny, A. Joachimiak and L. Hedstrom

Synopsis: Compound P131 displays antiparasitic activity in a mouse model of Cryptosporidium infection, validating IMP dehydrogenase (IMPDH) as a drug target. Here, the structure of the enzyme-substrate-P131 complex is reported at 2.05 Å resolution. The structure is an important step to further refine the design of IMPDH inhibitors.

Accepted 29 December 2014

Structure of a CutA1 divalent-cation tolerance protein from Cryptosporidium parvum, the protozoal parasite responsible for cryptosporidiosis

G. W. Buchko, J. Abendroth, M. C. Clifton, H. Robinson, Y. Zhang, S. N. Hewitt, B. L. Staker, T. E. Edwards, W. C. Van Voorhis and P. J. Myler

Synopsis: C. parvum is the primary protozoan parasite from the Cryptosporidium genus responsible for cryptosporidiosis in humans. Here, the 2.0 Å resolution structure of the divalent-cation tolerance protein CutA1 encoded in the genome of C. parvum Iowa II is described.

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