Acta Crystallographica Section F is a rapid structural biology communications journal.

Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal.

The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles.

Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.

Acta Crystallographica Section F is a rapid communications journal focused on structural biology. The journal welcomes articles on all aspects of structural biology, including structures determined using high-throughput methods or iterative studies commonly employed in the pharmaceutical industry. It offers an open access option, allowing unlimited free use of color illustrations without page charges. Authors are encouraged to submit multimedia content alongside their articles. Additionally, Acta Crystallographica Section F features a dedicated online tool called publBio, designed to facilitate the preparation and submission of articles for authors.

《Acta Crystallographica Section F: Structural Biology and Crystallization Communications》是一本快速发表结构生物学通讯的期刊。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或制药行业中常用的迭代研究所确定的结构。期刊提供开放获取选项，所有通讯均可无限制免费使用彩色插图，并且没有页面费用。鼓励作者提交多媒体内容与文章一同发表。《Acta Crystallographica Section F》还提供了一个名为publBio的在线工具，旨在简化作者的文章准备和提交过程。

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Histidine triad nucleotide-binding protein 2 (HINT2) is a mitochondrial adenosine phosphoramidase mainly expressed in the pancreas, liver and adrenal gland. HINT2 possibly plays a role in apoptosis, as well as being involved in steroid biosynthesis, hepatic lipid metabolism and regulation of hepatic mitochondria function. The expression level of HINT2 is significantly down-regulated in hepatocellular carcinoma patients. To date, endogenous substrates for this enzyme, as well as the three-dimensional structure of human HINT2, are unknown. In this study, human HINT2 was cloned, overexpressed in Escherichia coli and purified. Crystallization was performed at 278 K using PEG 4000 as the main precipitant; the crystals, which belonged to the tetragonal space group P41212 with unit-cell parameters a = b = 76.38, c = 133.25 Å, diffracted to 2.83 Å resolution. Assuming two molecules in the asymmetric unit, the Matthews coefficient and the solvent content were calculated to be 2.63 Å(3) Da(-1) and 53.27%, respectively.

Rafał Dolot

Artur Włodarczyk

Grzegorz D. Bujacz

Barbara Nawrot

Acta Crystallographica Section F Structural Biology and Crystallization Communications

Acta Cryst Sect F

Expression, purification, crystallization and preliminary X-ray crystallographic analysis of human histidine triad nucleotide-binding protein 2 (hHINT2)

人组氨酸三联核苷酸结合蛋白2（hHINT2）的表达、纯化、结晶及初步X射线晶体学分析

GluB is a substrate-binding protein (SBP) which participates in the uptake of glutamic acid in Corynebacterium glutamicum, a Gram-positive bacterium. It is part of an ATP-binding cassette (ABC) transporter system. Together with the transmembrane proteins GluC and GluD and the cytoplasmic protein GluA, which couples the hydrolysis of ATP to the translocation of glutamate, they form a highly active glutamate-uptake system. As part of efforts to study the amino-acid metabolism, especially the metabolism of glutamic acid by C. glutamicum, a bacterium that is widely used in the industrial production of glutamic acid, the GluB protein was expressed, purified and crystallized, an X-ray diffraction data set was collected to a resolution of 1.9 Å and preliminary crystallographic analysis was performed. The crystal belonged to space group P3121 or P3221, with unit-cell parameters a = b = 82.50, c = 72.69 Å.

Qingbo Liu

Defeng Li

Yonglin Hu

Da-Cheng Wang

Expression, crystallization and preliminary crystallographic study of GluB fromCorynebacterium glutamicum

谷氨酸棒杆菌GluB的表达、结晶及初步晶体学研究

Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their corresponding aldehydes, with the concomitant reduction of O2 to H2O2. Catalysis requires two cofactors: a mononuclear copper center and the cofactor 2,4,5-trihydroxyphenylalanine quinone (TPQ). TPQ is synthesized through the post-translational modification of an endogenous tyrosine residue and requires only oxygen and copper to proceed. TPQ biogenesis in CAO can be supported by alternate metals, albeit at decreased rates. A variety of factors are thought to contribute to the degree to which a metal can support TPQ biogenesis, including Lewis acidity, redox potential and electrostatic stabilization capability. The crystal structure has been solved of one of two characterized CAOs from the yeast Hansenula polymorpha (HPAO-1) in its metal-free (apo) form, which contains an unmodified precursor tyrosine residue instead of fully processed TPQ (HPAO-1 was denoted HPAO in the literature prior to 2010). Structures of apoHPAO-1 in complex with CuI and CoII have also been solved, providing structural insight into metal binding prior to biogenesis.

Valerie J. Klema

Bryan J. Johnson

Judith P. Klinman

Carrie M. Wilmot

The precursor form ofHansenula polymorphacopper amine oxidase 1 in complex with CuIand CoII

汉森酵母铜胺氧化酶1的前体形式与CuI和CoII的复合物

The structure of a newly crystallized form of the copper-dependent amine oxidase from pea seedlings has been refined at a resolution of 2.2 Å to a final R factor of 0.181. The structure (form II) was originally discovered during a study of xenon binding to copper-dependent amine oxidases as a probe for dioxygen-binding sites [Duff et al. (2004), J. Mol. Biol. 344, 599–607]. The form II crystals belong to space group P21, with two dimers in the asymmetric unit. The overall structure is very similar to the crystals of form I in space group P212121 with a dimer in the asymmetric unit [Kumar et al. (1996), Structure, 4, 943–955]. In form I the last three residues (644–647) observable in the two subunits were apparently splayed apart. It was noted that the absence of a disulfide bond between the Cys647 residues of the two subunits was inconsistent with chemical evidence for the absence of free sulfhydryl groups. In both of the crystallographically independent dimers of form II the two subunits are clearly joined by a disulfide bridge between the C-terminal cysteine residues. This is only possible if the two polypeptide chains in the dimer adopt different conformations near the C-terminus so that the twofold symmetry is lost. A proline residue (645) two residues before the cysteine has a cis conformation in one chain and a trans conformation in the other. As a result, the disulfide bond lies more than 5 Å from the twofold axis. The loss of local twofold symmetry in form II can be explained by intermolecular contacts, which provide an asymmetric environment.

Anthony P. Duff

Eric M. Shepard

David B. Langley

David M. Dooley

Hans C. Freeman

J. Mitchell Guss

A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer

豌豆幼苗中含铜胺氧化酶的C端二硫键破坏了分子二聚体的二重对称性

Complexes of Arthrobacter globiformis amine oxidase (AGAO) with the inhibitors benzylhydrazine and tranylcypromine (an antidepressant drug) have been refined at 1.86 and 1.65 Å resolution, respectively. Both inhibitors form covalent adducts with the TPQ cofactor. A tyrosine residue, proposed to act as a gate to the AGAO active site, is in its open conformation.

Daniel M. Trambaiolo

Complexes of the copper-containing amine oxidase fromArthrobacter globiformiswith the inhibitors benzylhydrazine and tranylcypromine

来自Arthrobacter globiformis的含铜胺氧化酶与抑制剂苄基肼和反式环丙胺的复合物

The coming year 2014 will be an important year for crystallography as the scientific community throughout the world celebrates the International Year of Crystallography.Acta Cryst.F will commemorate this special event with a series of articles defining the current state-of-the-art in macromolecular crystallization, with one article appearing per month throughout 2014 and into 2015.We expect this series to be a useful resource for our readership and the wider structural biology community alike.Stay tuned.We have also been working diligently over the past two or three years to finalize new requirements and a new format for our regular articles.Maybe some of you have attended the presentations given by us at various meetings or workshops about the publication tool publBio (http://publbio.iucr.org).publBio is designed to make the preparation and submission of an article much more simple and straightforward than ever before, be it a structural or a crystallization communication.The latest version not only guides authors through the requirements for each article type but also provides a means of submitting the article directly to Acta Cryst.F, thus simplifying the first stages of the submission process.The IUCr Word template now also has some of the functionality of publBio and, just like publBio, offers the option of utilizing data from an existing PDB deposition or an mmCIF file when creating the tables in your article.In July this year, we published a contribution by Janet Newman and colleagues entitled Crystallization reports are the backbone of Acta F, but do they have any spine?(Newman et al., 2013;Weiss & Einspahr, 2013).The central message of this paper was that the information content of crystallization communications published in Acta Cryst.F varies widely.While this may not seem troubling at first glance, the notion that as many as 60% of these articles lack some essential information sparked some concern.With publBio, we have a tool that will allow us to address this issue efficiently and effectively, and that will also make a major contribution to correcting the problem.We feel that the time has come to take advantage of this by making publBio (or its counterpart in the IUCr Word template) mandatory for writing and submitting crystallization communications from 1 January 2014.We expect that you will enjoy working with publBio and we are looking forward to working with you to refine and improve it.From our perspective, another major advance is that publBio will make clear exactly what data are needed for an acceptable crystallization communication.There will of course be situations in which certain data items may not be necessary or may be unavailable, but these 'exceptions to the rules' are exactly those about which authors need to confer with Co-editors.Therefore, we ask our authors to make full use of publBio to ease the burden of creating their publications.Finally, we thank our authors for their continued support of our journal and wish you all Season's Greetings and Happy Holidays.We look forward to 2014 with anticipation of all the new things this New Year will bring.

Manfred S. Weiss

Howard Einspahr

Big changes are ahead – a new format for crystallization communications inActa Cryst. F

重大变革即将到来——《Acta Cryst. F》结晶通讯新格式

The modular carbohydrate-active enzyme belonging to glycoside hydrolase family 30 (GH30) from Clostridium thermocellum (CtXynGH30) is a cellulosomal protein which plays an important role in plant cell-wall degradation. The full-length CtXynGH30 contains an N-terminal catalytic module (Xyn30A) followed by a family 6 carbohydrate-binding module (CBM6) and a dockerin at the C-terminus. The recombinant protein has a molecular mass of 45 kDa. Preliminary structural characterization was carried out on Xyn30A crystallized in different conditions. All tested crystals belonged to space group P1 with one molecule in the asymmetric unit. Molecular replacement has been used to solve the Xyn30A structure.

Anil Kumar Verma

Arun Goyal

Filipe Freire

Pedro Bule

Immacolata Venditto

Joana L. A. Brás

Helena Santos

Vânia Cardoso

Cecília Bonifácio

Andrew Thompson

Maria João Romão

José A. M. Prates

Luís M. A. Ferreira

Carlos M. G. A. Fontes

Shabir Najmudin

Overexpression, crystallization and preliminary X-ray crystallographic analysis of glucuronoxylan xylanohydrolase (Xyn30A) fromClostridium thermocellum

过表达、结晶及来自热纤维梭菌的木聚糖酶（Xyn30A）的初步X射线晶体学分析

The Escherichia coli cyclic AMP receptor protein (CRP) is a prokaryotic global transcription activator protein that controls the expression of many different genes. Wild-type CRP can bind to special DNA sequences in the presence of cAMP. The substitution of Asp53 by His results in the CRP* phenotype, which does not require exogenous cAMP. In the present study, the D53H CRP mutant was overexpressed, purified and crystallized. cAMP-free D53H CRP crystals were obtained and diffracted to a resolution of 2.9 Å. Based on the systematic absences of the crystals, the space group is likely to be P212121, with unit-cell parameters a = 76.66, b = 152.14, c = 176.11 Å. The asymmetric unit was confirmed to contain four protein dimers, with a Matthews coefficient of 2.71 Å3 Da−1 and a solvent content of 54.68%.

Jing Huang

Tong Wu

Zheng Guo

Tiantian Lou

Shaoning Yu

Weimin Gong

Chaoneng Ji

Crystallization and preliminary X-ray diffraction analysis of D53H mutantEscherichia colicAMP receptor protein

D53H突变型大肠杆菌cAMP受体蛋白的结晶及初步X射线衍射分析

Adenovirus fibre proteins play an important role in determining viral tropism. The C-terminal domain of the fibre protein from snake adenovirus type 1, a member of the Atadenovirus genus, has been expressed, purified and crystallized. Crystals were obtained belonging to space groups P212121 (two different forms), I213 and F23. The best of these diffracted synchrotron radiation to a resolution of 1.4 Å. As the protein lacks methionines or cysteines, site-directed mutagenesis was performed to change two leucine residues to methionines. Crystals of selenomethionine-derivatized crystals of the I213 form were also obtained and a multi-wavelength anomalous dispersion data set was collected.

Abhimanyu K. Singh

Rosa Menéndez-Conejero

Carmen San Martín

Mark J. van Raaij

Crystallization of the C-terminal domain of the fibre protein from snake adenovirus 1, an atadenovirus

蛇腺病毒1纤维蛋白C端结构域的结晶，一种腺病毒

The response-regulatory protein LytR belongs to a family of transcription factors involved in the regulation of important virulence factors in pathogenic bacteria. The protein consists of a receiver domain and an effector domain, which play an important role in controlled cell death and lysis. The LytR receiver domain (LytRN) has been overexpressed, purified and crystallized using the sitting-drop and hanging-drop vapour-diffusion methods. The crystals grew as needles, with unit-cell parameters a = b = 84.82, c = 157.3 Å, α = β = 90, γ = 120°. LytRN crystallized in space group P6122 and the crystals diffracted to a maximum resolution of 2.34 Å. Based on the Matthews coefficient (VM = 5.44 Å3 Da−1), one molecule is estimated to be present in the asymmetric unit.

Agnesa Shala

Kevin H. Patel

Dasantila Golemi-Kotra

Gerald F. Audette

Expression, purification, crystallization and preliminary X-ray analysis of the receiver domain ofStaphylococcus aureusLytR protein

金黄色葡萄球菌LytR蛋白接收域的表达、纯化、结晶及初步X射线分析

Publication Information	Publisher: Wiley-Blackwell Publishing Ltd，Publishing cycle: Monthly，Journal Type: journal，Open Access Journals: No
Basic data	Year of publication: 2005，Proportion of original research papers: 98.04%，Self Citation Rate:0.00%， Gold OA Rate: 46.31%
Average review cycle	网友分享经验：较快,2-4周
Average recruitment ratio	网友分享经验：容易

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

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