ACTA CRYSTALLOGRAPHICA SECTION F 是一本快速结构生物学通讯期刊。该期刊欢迎有关结构生物学任何方面的文章，包括使用高通量方法确定的结构或来自诸如制药行业使用的迭代研究的结构。该期刊提供开放访问选项和所有通信都受益于无限制免费使用彩色插图且不收取页面费用。鼓励作者提交多媒体内容以与他们的文章一起发表。ACTA CRYST。 F 有一个名为 PUBLBIO 的专用在线工具，旨在使作者更轻松地准备和提交文章。

Acta Crystallographica Section F: Structural Biology Communications is a rapid communications journal dedicated to structural biology research. The journal welcomes articles on all aspects of structural biology, including structures determined using high-throughput methods or those derived from iterative studies in the pharmaceutical industry. It offers open access options, and all communications benefit from unlimited free use of color illustrations without page charges. Authors are encouraged to submit multimedia content to accompany their articles. Additionally, Acta Crystallographica Section F provides a dedicated online tool called PUBLBIO, designed to assist authors in preparing and submitting their manuscripts more easily.

《Acta Crystallographica Section F: Structural Biology Communications》是一本快速发表结构生物学研究成果的通讯期刊。该期刊欢迎关于结构生物学各个方面的文章，包括使用高通量方法获得的结构，或来自制药行业的迭代研究所产生的结构。期刊提供开放获取选项，所有通信均可无限制免费使用彩色插图，且不收取页面费用。我们鼓励作者提交多媒体内容以与文章一同发表。此外，《Acta Crystallographica Section F》还提供名为PUBLBIO的专用在线工具，旨在帮助作者更轻松地准备和提交文章。

Acta Crystallographica Section F:Structural Biology Communications

Plasmodium vivax , a significant contributor to global malaria cases, poses an escalating health burden on a substantial portion of the world's population. The increasing spread of P. vivax because of climate change underscores the development of new and rational drug-discovery approaches. The Seattle Structural Genomics Center for Infectious Diseases is taking a structure-based approach by investigating essential enzymes such as N -myristoyltransferase (NMT). P. vivax N -myristoyltransferase ( Pv NMT) is a promising target for the development of novel malaria treatments unlike current drugs, which target only the erythrocytic stages of the parasite. Here, the 1.8 Å resolution ternary structure of Pv NMT in complex with myristoyl-CoA and IMP-1088, a validated NMT inhibitor, is reported. IMP-1088 is a validated nonpeptidic inhibitor and a ternary complex structure with human NMT has previously been reported. IMP-1088 binds similarly to Pv NMT as to human NMT.

Alex Mendez

Cydni Bolling

Shane Taylor

Stanley Makumire

Bart Staker

Alexandra Reers

Brad Hammerson

Stephen J Mayclin

Jan Abendroth

Donald D Lorimer

Thomas E Edwards

Edward W Tate

Sandhya Subramanian

Andrew S Bell

Peter J Myler

Oluwatoyin A Asojo

Graham Chakafana

Acta Crystallographica Section F Structural Biology Communications

Structure of Plasmodium vivax N-myristoyltransferase with inhibitor IMP-1088: exploring an NMT inhibitor for antimalarial therapy

Plasmodium vivax N-肉豆蔻酰转移酶与抑制剂IMP-1088的结构：探索用于抗疟治疗的NMT抑制剂

The resistance of the emerging human pathogen Stenotrophomonas maltophilia to tetracycline antibiotics mainly depends on multidrug efflux pumps and ribosomal protection enzymes. However, the genomes of several strains of this Gram-negative bacterium code for a FAD-dependent monooxygenase (SmTetX) homologous to tetracycline destructases. This protein was recombinantly produced and its structure and function were investigated. Activity assays using SmTetX showed its ability to modify oxytetracycline with a catalytic rate comparable to those of other destructases. SmTetX shares its fold with the tetracycline destructase TetX from Bacteroides thetaiotaomicron; however, its active site possesses an aromatic region that is unique in this enzyme family. A docking study confirmed tetracycline and its analogues to be the preferred binders amongst various classes of antibiotics.

Martin Malý

Petr Kolenko

Jan Stránský

Leona Švecová

Jarmila Dušková

Tomáš Koval'

Tereza Skálová

Mária Trundová

Kristýna Adámková

Jiří Černý

Paulína Božíková

Jan Dohnálek

Tetracycline-modifying enzymeSmTetX fromStenotrophomonas maltophilia

来自嗜麦芽窄食单胞菌的四环素修饰酶SmTetX

This study reports the successful replacement of uranyl-based stains by either sodium phosphotungstate or ammonium molybdate in negative-staining electron microscopy. Using apoferritin as a test specimen, it is demonstrated that in combination with a facile on-grid fixation step, both stains yield comparable images to uranyl formate. Subsequently, using β-galactosidase, it is shown that both stains can also successfully be employed for single-particle analysis, yielding virtually indistinguishable results from uranyl formate. As both replacement stains are nonradioactive, they are not subjected to the same handling restrictions as uranyl-based stains. Therefore they are not only cheaper to use, but also make decentralized sample-grid preparation, directly after purification, accessible to a broader range of scientists.

Monika Gunkel

Arthur Macha

Elmar Behrmann

Revisiting sodium phosphotungstate and ammonium molybdate as nonradioactive negative-staining agents for single-particle analysis

重访磷钨酸钠和钼酸铵作为单颗粒分析的非放射性负染色剂

Helicobacter pylori is one of the most common bacterial infections; over two-thirds of the world's population is infected by early childhood. Persistent H. pylori infection results in gastric ulcers and cancers. Due to drug resistance, there is a need to develop alternative treatments to clear H. pylori . The Seattle Structural Genomics Center for Infectious Disease (SSGCID) conducts structure–function analysis of potential therapeutic targets from H. pylori . Glutamyl-tRNA synthetase (GluRS) is essential for tRNA aminoacylation and is under investigation as a bacterial drug target. The SSGCID produced, crystallized and determined the apo structure of H. pylori GluRS ( Hp GluRS). Hp GluRS has the prototypical bacterial GluRS topology and has similar binding sites and tertiary structures to other bacterial GluRS that are promising drug targets. Residues involved in glutamate binding are well conserved in comparison with Pseudomonas aeruginosa GluRS ( Pa GluRS), which has been studied to develop promising new inhibitors for P. aeruginosa . These structural similarities can be exploited for drug discovery and repurposing to generate new antibacterials to clear persistent H. pylori infection and reduce gastric ulcers and cancer.

Dylan E. Davis

Jesuferanmi P. Ayanlade

David T. Laseinde

Hannah Udell

Donald J. Lorimer

David M. Dranow

Thomas E. Edwards

Peter J. Myler

Oluwatoyin A. Asojo

Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori

幽门螺杆菌谷氨酰-tRNA合成酶的晶体结构

The unicellular parasitic protozoan Trichomonas vaginalis causes trichomoniasis, the most prevalent nonviral sexually transmitted disease globally. T. vaginalis evades host immune responses by producing homologs of host proteins, including cytokines such as macrophage migration inhibitory factor. T. vaginalis macrophage migration inhibitory factor ( Tv MIF) helps to facilitate the survival of T. vaginalis during nutritional stress conditions, increases prostate cell proliferation and invasiveness, and induces inflammation-related cellular pathways, thus mimicking the ability of human MIF to increase inflammation and cell proliferation. The production, crystallization and three structures of N-terminally hexahistidine-tagged Tv MIF reveal a prototypical MIF trimer with a topology similar to that of human homologs (hMIF-1 and hMIF-2). The N-terminal tag obscures the expected pyruvate-binding site. The similarity of Tv MIF to its human homologs can be exploited for structure-based drug discovery.

Aruesha Srivastava

Aryana Nair

Omolara C. O. Dawson

Raymond Gao

Lijun Liu

Justin K. Craig

Kevin P. Battaile

Elizabeth K. Harmon

Lynn K. Barrett

Wesley C. Van Voorhis

Scott Lovell

Rabih Darwiche

Structures of Trichomonas vaginalis macrophage migratory inhibitory factor

Trichomonas vaginalis巨噬细胞移动抑制因子的结构

Burkholderia cenocepacia is an opportunistic human pathogen that can cause lethal infections in immunocompromised individuals, particularly those with cystic fibrosis. As such, there is a critical need to identify and characterize the structure and function of enzymes that participate in the metabolic pathways of this bacterium. Here, the high-resolution X-ray crystal structure of a short-chain dehydrogenase reductase (SDR) from B. cenocepacia J2315 (BcSDR) in complex with the coenzyme NADP + and a benzoic acid ligand is presented. This protein has the conserved Rossmann fold of the SDR superfamily and the characteristic TG xxx G x G motif of the classical SDR subfamily. However, unlike classical SDRs, the active site of BcSDR has a leucine residue in place of the highly conserved and catalytically important tyrosine residue. Sequence analysis confirms that this leucine residue is conserved in this SDR across the Burkholderiales order. This suggests that BcSDR is more appropriately classified into the divergent SDR subfamily. In addition, this enzyme would necessarily employ a different enzyme mechanism to that proposed as a general mechanism for most SDRs.

Kafi K. J. Belfon

Olive Beyer

Donald D. Lorimer

Ariel Abramov

Yazmine Latimore

Connor Hamilton

Aniah Dawkins

Isabella Hinojosa

Xavier Martinez

Sofia Mirabel

Miriam Duncan

Reagan Womack

Lillian Hicks

Zachary R. Turlington

Andrew T. Torelli

Katherine A. Hicks

Jarrod B. French

Crystal structure of a short-chain dehydrogenase from Burkholderia cenocepacia J2315 in complex with NADP+ and benzoic acid

来自Burkholderia cenocepacia J2315的短链脱氢酶与NADP+和苯甲酸复合物的晶体结构

Abbreviation	Acta Cryst Sect F
Journal Impact	0.93
Quartiles(Global)	CRYSTALLOGRAPHY(Q3)

ISSN	2053-230X
h-index	44

Publication Information	Publisher: John Wiley and Sons Ltd，Publishing cycle: ，Journal Type: journal，Open Access Journals: No
Basic data	Year of publication: 2014，Proportion of original research papers: 98.04%，Self Citation Rate:0.00%， Gold OA Rate: 46.31%

Acta Crystallographica Section F:Structural Biology Communications

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Structure of Plasmodium vivax N-myristoyltransferase with inhibitor IMP-1088: exploring an NMT inhibitor for antimalarial therapy

Tetracycline-modifying enzymeSmTetX fromStenotrophomonas maltophilia

Revisiting sodium phosphotungstate and ammonium molybdate as nonradioactive negative-staining agents for single-particle analysis

Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori

Structures of Trichomonas vaginalis macrophage migratory inhibitory factor

Structure of Plasmodium vivax N-myristoyltransferase with inhibitor IMP-1088: exploring an NMT inhibitor for antimalarial therapy

Crystal structure of a short-chain dehydrogenase from Burkholderia cenocepacia J2315 in complex with NADP⁺ and benzoic acid

Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori

Structures of Trichomonas vaginalis macrophage migratory inhibitory factor

Revisiting sodium phosphotungstate and ammonium molybdate as nonradioactive negative-staining agents for single-particle analysis