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.

A strategy for selecting the pH of protein solutions to enhance crystallization

C.-Y. Zhang, Z.-Q. Wu, D.-C. Yin, B.-R. Zhou, Y.-Z. Guo, H.-M. Lu, R.-B. Zhou and P. Shang

Crystallization and preliminary crystallographic analysis of Abp, a GH27 -L-arabinopyranosidase from Geobacillus stearothermophilus

S. Lansky, R. Salama, V. Solomon, H. Belrhali, Y. Shoham and G. Shoham

Synopsis: A GH27 arabinopyranosidase from G. stearothermophilus (Abp) has been crystallized in the primitive orthorhombic space group P2₁2₁2₁. Full diffraction data sets have been measured for the wild-type enzyme and its D197A catalytic mutant to a maximal resolutions of 2.28 and 2.3 Å, respectively, for use in a detailed three-dimensional structural analysis of the Abp protein.

Crystallization and preliminary X-ray diffraction analysis of tetrathionate hydrolase from Acidithiobacillus ferrooxidans

T. Kanao, M. Kosaka, K. Yoshida, H. Nakayama, T. Tamada, R. Kuroki, H. Yamada, J. Takada and K. Kamimura

Synopsis: The recombinant tetrathionate hydrolase from the acidophilic chemolithoautotrophic bacterium A. ferrooxidans was refolded for activation, purified and crystallized. Diffraction data were collected to 2.15 Å resolution.

ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family

J. J. E. Caesar, S. Johnson, P. Kraiczy and S. M. Lea

Synopsis: The structure of ErpC, a member of the complement regulator-acquiring surface protein family from B. burgdorferi, has been solved, providing insights into the strategies of complement evasion by this zoonotic bacterium and suggesting a common architecture for other members of this protein family.

Expression, purification, crystallization and preliminary X-ray crystallographic study of the nucleocapsid protein of Tomato spotted wilt virus

K. Komoda, M. Narita, I. Tanaka and M. Yao

Preliminary crystallographic analysis of neuraminidase N2 from a new influenza A virus

F. Gao and J. Bao

Synopsis: The preliminary crystallographic analysis of neuraminidase N2 from influenza virus A/Myanmar/M187/2007 is reported. The crystals belonged to space group P2₁2₁2₁, with four monomers per asymmetric unit.

Structure of an A-form RNA duplex obtained by degradation of 6S RNA in a crystallization droplet

J. Kondo, A.-C. Dock-Bregeon, D. K. Willkomm, R. K. Hartmann and E. Westhof

Crystallographic analysis of new psychrophilic haloalkane dehalogenases: DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17

K. Tratsiak, O. Degtjarik, I. Drienovska, L. Chrast, P. Rezacova, M. Kuty, R. Chaloupkova, J. Damborsky and I. Kuta Smatanova

Synopsis: The novel haloalkane dehalogenases DpcA from P. cryohalolentis K5 and DmxA from Marinobacter sp. ELB17 were successfully crystallized and diffraction data were collected to resolutions of 1.05 and 2.49 Å, respectively.

Crystallization and preliminary X-ray diffraction analysis of the DNA-binding domain of the response regulator SaeR from Staphylococcus epidermidis

S.-C. Chen, C.-H. Huang, Y.-R. Chen, C. S. Yang, C.-T. Lin and Y. Chen

Synopsis: The DNA-binding domain of the response regulator SaeR was crystallized. Determination of its structure will reveal the residues that are critical for protein-DNA recognition.

Structure of PatF from Prochloron didemni

A. F. Bent, J. Koehnke, W. E. Houssen, M. C. M. Smith, M. Jaspars and J. H. Naismith

Synopsis: The X-ray crystal structure of PatF from P. didemni was solved by the single-wavelength anomalous diffraction method to a resolution of 2.13 Å.

Structure of diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase from Acinetobacter baumannii

A. Dawson, P. Trumper, G. Chrysostomou and W. N. Hunter

Synopsis: The structure of a bifunctional deaminase/reductase involved in riboflavin biosynthesis in the pathogen A. baumannii has been determined in two crystal forms.

Purification, crystallization and preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis DNA gyrase ATPase domain

M. Roué, A. Agrawal, C. Volker, D. Mossakowska, C. Mayer and B. D. Bax

Synopsis: The ATPase domain of M. tuberculosis DNA gyrase was crystallized using hanging-drop vapour diffusion. The crystals belonged to space groups P1 and P2₁. Diffraction data were collected to resolutions of 2.9 and 3.3 Å, respectively.

Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi

J. J. E. Caesar, R. Wallich, P. Kraiczy, P. F. Zipfel and S. M. Lea

Synopsis: B. burgdorferi binds complement factor H using a dimeric surface protein, CspA (BbCRASP-1). Presented here is a new structure of CspA that suggests that there is a degree of flexibility between subunits which may have implications for complement regulator binding.

Crystallization and preliminary X-ray diffraction analysis of a new xyloglucanase from Xanthomonas campestris pv. campestris

E. A. de Araújo, A. Tomazini, M. A. S. Kadowaki, M. T. Murakami and I. Polikarpov

Synopsis: X. campestris pv. campestris xyloglucanase was produced in E. coli using recombinant pSMT3 vector. Crystals were obtained and X-ray data sets were collected for both the apoenzyme and its complex with glucose.

Purification, crystallization and preliminary X-ray crystallographic study of the tRNA pseudouridine synthase TruB from Streptococcus pneumoniae

W. Yang, S. Zhao, L. Jin, Z. Guo, S. Zhang, H. Zhang and D. Wang

Crystallization and preliminary crystallographic analysis of recombinant hyaluronate lyase from Streptococcus suis

A. H. Khan, Y. M. Mohamed Omar, M. A. Kakar and N. Bangulzai

Structure of the T6SS lipoprotein TssJ1 from Pseudomonas aeruginosa

C. S. Robb, M. Assmus, F. E. Nano and A. B. Boraston

Synopsis: The crystal structure of the type VI secretion-system protein TssJ1 from P. aeruginosa was solved by iodide SAD at a resolution of 1.4 Å.

Expression, purification, crystallization and preliminary X-ray diffraction analysis of EtFPOX from Eupenicillium terrenum sp.

K. Xing, W. Gan, M. Jia, F. Gao and W. Gong

Synopsis: Crystals of EtFPOX from E. terrenum sp. diffracted to 1.9 Å resolution and belonged to space group P2₁2₁2₁, with unit-cell parameters a = 65.6, b = 80.0, c = 83.4 Å.

Heterogeneous nucleation helps the search for initial crystallization conditions of -glutamyl transpeptidase from Bacillus licheniformis

L.-L. Lin and A. Merlino

Synopsis: An additional example in which heterogeneous nucleation has helped in the search for crystallization conditions of a protein is reported. Optimization of the crystallization conditions led to the formation of single crystals of -glutamyl transpeptidase from B. licheniformis that diffracted to about 3.0 Å resolution.

Crystallization and preliminary X-ray analysis of the flagellar motor `brake' molecule YcgR with c-di-GMP from Escherichia coli

Y. Hou, D.-F. Li and D.-C. Wang

Synopsis: The flagellar motor `brake' protein YcgR from E. coli was crystallized with c-di-GMP. The crystals diffracted to 2.3 Å resolution and belonged to space group R3:H, with unit-cell parameters a = b = 93.96, c = 109.61 Å.

A triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interface

A. Lampel, O. Yaniv, O. Berger, E. Bacharach, E. Gazit and F. Frolow

Synopsis: The triclinic structure of the HIV-1 capsid protein contains four molecules in the asymmetric unit that form a novel packing interface that could conceivably resemble an intermediate structure that is involved in the early steps of HIV-1 assembly.

Expression, crystallization and preliminary crystallographic study of GluB from Corynebacterium glutamicum

Q. Liu, D. Li, Y. Hu and D.-C. Wang

Synopsis: GluB, a substrate-binding protein from C. glutamicum, was expressed, purified and crystallized, followed by X-ray diffraction data collection and preliminary crystallographic analysis.

Crystallization and preliminary X-ray study of a thermostable alanine racemase from Thermoanaerobacter tengcongensis MB4

H. Dong, S. Xu, X. Lu, G. He, R. Zhao, S. Chen, S. Fu and J. Ju

Synopsis: A thermostable alanine racemase from T. tengcongensis MB4 was expressed in E. coli and purified. Crystallization and preliminary X-ray crystallographic analysis were performed for the recombinant enzyme.

Crystallization and preliminary crystallographic studies of AAL-2, a novel lectin from Agrocybe aegerita that binds nonreducing terminal N-acetylglucosamine

X. Ren, S. Jiang, D. Li, H. Sun and D. Wang

Synopsis: AAL-2, an A. aegerita lectin that specifically recognizes nonreducing terminal acetylglucosamine, was crystallized and preliminary crystallographic studies were performed on this protein. This work provides a solid foundation for determination of the AAL-2 structure and illustration of the sugar-binding specificity of this novel lectin.

Crystallization of recombinant green mamba -Da1a toxin during a lyophilization procedure and its structure determination

A. Maïga, L. Vera, C. Marchetti, A. Lorphelin, L. Bellanger, G. Mourier, D. Servent, N. Gilles and E. A. Stura

Synopsis: Crystals of recombinantly expressed -Da1a toxin from eastern green mamba that were suitable for structure determination were discovered on defrosting a partially lyophilized sample.

Crystallization and X-ray diffraction analysis of an antifungal laticifer protein

F. Bruno-Moreno, R. Sombra Basílio de Oliveira, R. de Azevedo Moreira, M. D. Pinto Lobo, C. D. Teixeira de Freitas, M. Viana Ramos, T. Barbosa Grangeiro and A. C. Oliveira Monteiro-Moreira

Cloning, expression, crystallization and preliminary structural studies of dihydrodipicolinate reductase from Acinetobacter baumannii

S. Kaushik, A. Singh, M. Sinha, P. Kaur, S. Sharma and T. P. Singh

Crystal-contact engineering to obtain a crystal form of the Kelch domain of human Keap1 suitable for ligand-soaking experiments

S. Hörer, D. Reinert, K. Ostmann, Y. Hoevels and H. Nar

Synopsis: A mutant of the Kelch domain of the human Keap1 protein has been designed in order to enable the soaking of small-molecule ligands. The apo structure of this mutant is reported at 1.98 Å resolution and the suitability of the crystal system has been demonstrated by the structure of the mutated Keap1 Kelch domain in complex with a cyclic peptide derived from Nrf2.

Crystallization and preliminary structural analysis of dibenzothiophene monooxygenase (DszC) from Rhodococcus erythropolis

X. Duan, L. Zhang, D. Zhou, K. Ji, T. Ma, W. Shui, G. Li and X. Li

Synopsis: The structure of DszC from R. erythropolis DS-3 was solved using the single-wavelength anomalous dispersion method.

Crystallization and preliminary X-ray crystallographic analysis of the rhesus macaque MHC class I molecule Mamu-B*17 complexed with an immunodominant SIVmac239 Env epitope

F. Gao and J. Bao

Synopsis: A primitive monoclinic crystal of the rhesus macaque MHC class I molecule Mamu-B*17 complexed with an SIVmac239 Env peptide was obtained and belonged to space group P2, with unit-cell parameters a = 68.3, b = 45.0, c = 81.5 Å, = 96.5°. The crystal diffracted to 2.55 Å resolution.

Purification, crystallization and preliminary crystallographic analysis of the 23S rRNA methyltransferase RlmM (Cm2498) from Escherichia coli

H.-Y. Guo, Z.-Q. Gao, H. Zhang, Y. Wei, J.-H. Xu, A. Yan and Y.-H. Dong

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