Acta Crystallographica Section F-structural Biology and Crystallization Communications最新文献_第10页

A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus. 金黄色葡萄球菌 3-甲基腺嘌呤 DNA 糖基化酶 I (TAG) 识别 3-甲基腺嘌呤的模型。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-22 DOI: 10.1107/S1744309112016363

Xiaofeng Zhu, Xuan Yan, Lester G Carter, Huanting Liu, Shirley Graham, Peter J Coote, James Naismith

引用次数: 0

Purification, crystallization and preliminary X-ray analysis of nonstructural protein 2 (nsp2) from avian infectious bronchitis virus. 禽传染性支气管炎病毒非结构蛋白2 (nsp2)的纯化、结晶及x射线初步分析。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-24 DOI: 10.1107/S1744309112018623

Kun Yu, Zhenhua Ming, Yuanyuan Li, Cheng Chen, Zehua Bao, Zhilin Ren, Bofeng Liu, Wei Tao, Zihe Rao, Zhiyong Lou

{"title":"Purification, crystallization and preliminary X-ray analysis of nonstructural protein 2 (nsp2) from avian infectious bronchitis virus.","authors":"Kun Yu, Zhenhua Ming, Yuanyuan Li, Cheng Chen, Zehua Bao, Zhilin Ren, Bofeng Liu, Wei Tao, Zihe Rao, Zhiyong Lou","doi":"10.1107/S1744309112018623","DOIUrl":"https://doi.org/10.1107/S1744309112018623","url":null,"abstract":"Avian infectious bronchitis virus (IBV) is a member of the group III coronaviruses, which differ from the other groups of coronaviruses in that they do not encode the essential pathogenic factor nonstructural protein 1 (nsp1) and instead start with nsp2. IBV nsp2 is one of the first replicase proteins to be translated and processed in the viral life cycle; however, it has an entirely unknown function. In order to better understand the structural details and functional mechanism of IBV nsp2, the recombinant protein was cloned, overexpressed in Escherichia coli, purified and crystallized. The crystals diffracted to 2.8 Å resolution and belonged to space group P2(1), with unit-cell parameters a = 57.0, b = 192.3, c = 105.7 Å, β = 90.8°. Two molecules were found in the asymmetric unit; the Matthews coefficient was 3.9 Å(3) Da(-1), corresponding to a solvent content of 68.2%.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"716-9"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309112018623","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30679348","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 11

Purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal fragment of the MvfR protein from Pseudomonas aeruginosa. 铜绿假单胞菌MvfR蛋白c端片段的纯化、结晶和初步x射线衍射分析。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-23 DOI: 10.1107/S1744309112016661

Katerina Kefala, Dina Kotsifaki, Mary Providaki, Evangelia G Kapetaniou, Lawrence Rahme, Michael Kokkinidis

引用次数: 11

Overexpression, purification, crystallization and preliminary X-ray analysis of putative molybdenum cofactor biosynthesis protein C (MoaC2) from Mycobacterium tuberculosis H37Rv. 结核分枝杆菌 H37Rv 中推测的钼辅助因子生物合成蛋白 C (MoaC2) 的过表达、纯化、结晶和初步 X 射线分析。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-23 DOI: 10.1107/S174430911201665X

Shubhra Srivastava, Vijay Kumar Srivastava, Ashish Arora, J Venkatesh Pratap

{"title":"Overexpression, purification, crystallization and preliminary X-ray analysis of putative molybdenum cofactor biosynthesis protein C (MoaC2) from Mycobacterium tuberculosis H37Rv.","authors":"Shubhra Srivastava, Vijay Kumar Srivastava, Ashish Arora, J Venkatesh Pratap","doi":"10.1107/S174430911201665X","DOIUrl":"10.1107/S174430911201665X","url":null,"abstract":"Rv0864 (MoaC2) from Mycobacterium tuberculosis is one of the enzymes in the molybdenum cofactor (Moco) biosynthesis pathway. Together with MoaA, MoaC is involved in the conversion of guanosine triphosphate (GTP) to precursor Z, the first step in Moco synthesis. Full-length MoaC2 (17.5 kDa, 167 residues) was cloned in Escherichia coli and purified to homogeneity. Crystals of recombinant M. tuberculosis MoaC2 were grown by vapour diffusion using a hanging-drop setup. Diffracting crystals grew in a condition in which 3 µl protein solution at 10.5 mg ml(-1) was mixed with 1.5 µl reservoir solution (0.025 M potassium sodium tartrate tetrahydrate pH 8.0) and equilibrated against 1000 µl reservoir solution. Diffraction data extending to 2.5 Å resolution were collected at 100 K. The crystal belonged to the cubic space group P2(1)3, with unit-cell parameter 94.5 Å. Matthews coefficient (V(M)) calculations suggested the presence of two molecules in the asymmetric unit, corresponding to a solvent content of about 39%. Molecular-replacement calculations using the E. coli homologue as the search model gave an unambiguous solution.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"687-91"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370911/pdf/f-68-00687.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30679379","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Crystallization and preliminary X-ray crystallographic analysis of Thermotoga maritima CheA P3-P4-P5 domains in complex with CheW. 海洋热藻CheA P3-P4-P5结构域与CheW配合物的结晶及初步x射线晶体学分析。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-24 DOI: 10.1107/S174430911201826X

Sangyoun Park, Keon Young Kim, Sunmin Kim, Brian R Crane

引用次数: 0

Crystallization and preliminary crystallographic studies of both components of the staphylococcal LukE-LukD leukotoxin. 葡萄球菌LukE-LukD白毒素两种成分的结晶和初步结晶学研究。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-23 DOI: 10.1107/S1744309112014662

Romain Galy, Fabien Bergeret, Daniel Keller, Lionel Mourey, Gilles Prévost, Laurent Maveyraud

{"title":"Crystallization and preliminary crystallographic studies of both components of the staphylococcal LukE-LukD leukotoxin.","authors":"Romain Galy, Fabien Bergeret, Daniel Keller, Lionel Mourey, Gilles Prévost, Laurent Maveyraud","doi":"10.1107/S1744309112014662","DOIUrl":"10.1107/S1744309112014662","url":null,"abstract":"Soluble forms of recombinant LukE protein (expressed in Escherichia coli) and of wild-type LukD protein (expressed in Staphylococcus aureus), which together form the staphylococcal LukE-LukD leukotoxin, were purified to homogeneity and crystallized using the sitting-drop vapour-diffusion method. The crystals of LukE belonged to space group I4, with unit-cell parameters a = b = 134.50, c = 64.43 Å, and diffracted X-rays to 1.6 Å resolution. The crystals of LukD belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 48.04, b = 50.99, c = 137.40 Å, and diffracted to 1.9 Å resolution. Molecular replacement using the LukF-PV structure (PDB entry 1pvl) as a template model allowed the identification of an initial structure solution for the LukD data. In the case of LukE, a solution comprising only a single copy of the search model (LukS-PV; PDB entry 1t5r) was found, although the unit-cell parameters indicated that up to three molecules could be accommodated in the asymmetric unit.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"663-7"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309112014662","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30681014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type III. 人肽精氨酸脱亚胺酶III型的结晶及初步x射线晶体学分析。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-23 DOI: 10.1107/S1744309112015333

Masaki Unno, Kenji Kizawa, Makiko Ishihara, Hidenari Takahara

引用次数: 10

Purification, crystallization and preliminary X-ray crystallographic analysis of the ATPase domain of human TAP in nucleotide-free and ADP-, vanadate- and azide-complexed forms. 人类 TAP 的 ATPase 结构域在无核苷酸和 ADP、钒酸盐及叠氮化物复合物形式下的纯化、结晶和初步 X 射线晶体学分析。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-23 DOI: 10.1107/S1744309112013954

Sita R Meena, Shanti P Gangwar, Ajay K Saxena

{"title":"Purification, crystallization and preliminary X-ray crystallographic analysis of the ATPase domain of human TAP in nucleotide-free and ADP-, vanadate- and azide-complexed forms.","authors":"Sita R Meena, Shanti P Gangwar, Ajay K Saxena","doi":"10.1107/S1744309112013954","DOIUrl":"10.1107/S1744309112013954","url":null,"abstract":"The human transporter associated with antigen processing (TAP) protein belongs to the ATP-binding cassette (ABC) transporter superfamily and is formed by the heterodimerization of TAP1 and TAP2 subunits. TAP selectively pumps cytosolic peptides into the lumen of the endoplasmic reticulum in an ATP-dependent manner. The catalytic cycle of the ATPase domain of TAP is not understood at the molecular level. The structures of catalytic intermediates of the ATPase domain of TAP will contribute to the understanding of the chemical mechanism of ATP hydrolysis. In order to understand this mechanism, the ATPase domain of human TAP1 (NBD1) was expressed and purified, crystallized in nucleotide-free and transition-state complex forms and X-ray crystallographic studies were performed. The NBD1 protein was crystallized (i) in the nucleotide-free apo form; (ii) in complex with ADP-Mg(2+), mimicking the product-bound state; (iii) in complex with vanadate-ADP-Mg(2+), mimicking the ATP-bound state; and (iv) in complex with azide-ADP-Mg(2+), also mimicking the ATP-bound state. X-ray diffraction data sets were collected for apo and complexed NBD1 using an in-house X-ray diffraction facility at a wavelength of 1.5418 Å. The apo and complexed NBD1 crystals belonged to the primitive hexagonal space group P6(2), with one monomer in the asymmetric unit. Here, the crystallization, data collection and preliminary crystallographic analysis of apo and complexed NBD1 are reported.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"655-8"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370903/pdf/f-68-00655.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30681012","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The ParE2-PaaA2 toxin-antitoxin complex from Escherichia coli O157 forms a heterodocecamer in solution and in the crystal. 来自大肠杆菌O157的ParE2-PaaA2毒素-抗毒素复合物在溶液和晶体中形成异docecamer。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-25 DOI: 10.1107/S1744309112015230

Yann G J Sterckx, Abel Garcia-Pino, Sarah Haesaerts, Thomas Jové, Lieselotte Geerts, Viktor Sakellaris, Laurence Van Melderen, Remy Loris

{"title":"The ParE2-PaaA2 toxin-antitoxin complex from Escherichia coli O157 forms a heterodocecamer in solution and in the crystal.","authors":"Yann G J Sterckx, Abel Garcia-Pino, Sarah Haesaerts, Thomas Jové, Lieselotte Geerts, Viktor Sakellaris, Laurence Van Melderen, Remy Loris","doi":"10.1107/S1744309112015230","DOIUrl":"10.1107/S1744309112015230","url":null,"abstract":"Escherichia coli O157 paaR2-paaA2-parE2 constitutes a unique three-component toxin-antitoxin (TA) module encoding a toxin (ParE2) related to the classic parDE family but with an unrelated antitoxin called PaaA2. The complex between PaaA2 and ParE2 was purified and characterized by analytical gel filtration, dynamic light scattering and small-angle X-ray scattering. It consists of a particle with a radius of gyration of 3.95 nm and is likely to form a heterododecamer. Crystals of the ParE2-PaaA2 complex diffract to 3.8 Å resolution and belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 142.9, c = 87.5 Å. The asymmetric unit is consistent with a particle of around 125 kDa, which is compatible with the solution data. Therefore, the ParE2-PaaA2 complex is the largest toxin-antitoxin complex identified to date and its quaternary arrangement is likely to be of biological significance.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"724-9"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309112015230","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30679350","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 7

Expression, purification, crystallization and preliminary X-ray analysis of Plasmodium falciparum GTP:AMP phosphotransferase. 恶性疟原虫 GTP:AMP 磷酸转移酶的表达、纯化、结晶和初步 X 射线分析。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-23 DOI: 10.1107/S1744309112015862

Alan W L Law, Julien Lescar, Quan Hao, Masayo Kotaka

引用次数: 0