Acta Crystallographica Section F-structural Biology and Crystallization Communications最新文献_第9页

Cloning, purification, crystallization and preliminary X-ray studies of human α1-microglobulin. 人 α1-微球蛋白的克隆、纯化、结晶和初步 X 射线研究。

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/S1744309112016569

Yangli Zhang, Zengqiang Gao, Zhenzhen Zhang, Miao Luo, Ailong Huang, Yuhui Dong, Deqiang Wang

{"title":"Cloning, purification, crystallization and preliminary X-ray studies of human α1-microglobulin.","authors":"Yangli Zhang, Zengqiang Gao, Zhenzhen Zhang, Miao Luo, Ailong Huang, Yuhui Dong, Deqiang Wang","doi":"10.1107/S1744309112016569","DOIUrl":"10.1107/S1744309112016569","url":null,"abstract":"α(1)-Microglobulin (α(1)m) is one of the phylogenetically most widespread lipocalins and is distributed in various organs and tissues, including liver, heart, eye, kidney, brain, lung, pancreas and skeletal muscle. α(1)m has been found to exert multifarious functions, including interacting with IgA, albumin and prothrombin, binding strongly to haem and exhibiting reductase activity. Nevertheless, little structural information is available regarding these functions of α(1)m. Since determination of three-dimensional structure is a powerful means of functional characterization, X-ray crystallography was used to accomplish this task. Here, the expression, purification, crystallization and preliminary crystallographic analysis of human α(1)m are reported. The crystal belonged to space group P4(3), with unit-cell parameters a = b = 36.45, c = 112.68 Å, and diffracted to a resolution of 2.0 Å. The crystals are most likely to contain one molecule in the asymmetric unit, with a V(M) value of 1.63 Å(3) Da(-1).","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"692-4"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370912/pdf/f-68-00692.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30679380","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

Purification, crystallization and preliminary X-ray analysis of human histidine decarboxylase. 人组氨酸脱羧酶的纯化、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: 2012-05-23 DOI: 10.1107/S1744309112015692

Hirofumi Komori, Yoko Nitta, Hiroshi Ueno, Yoshiki Higuchi

引用次数: 9

Crystallization and preliminary X-ray crystallographic analysis of the Bag2 amino-terminal domain from Mus musculus. 麝香鹿 Bag2 氨基末端结构域的结晶和初步 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/S1744309112013267

Richard C Page, Zhen Xu, Joseph Amick, Jay C Nix, Saurav Misra

{"title":"Crystallization and preliminary X-ray crystallographic analysis of the Bag2 amino-terminal domain from Mus musculus.","authors":"Richard C Page, Zhen Xu, Joseph Amick, Jay C Nix, Saurav Misra","doi":"10.1107/S1744309112013267","DOIUrl":"10.1107/S1744309112013267","url":null,"abstract":"Bag2, an atypical member of the Bag family of Hsp70 co-chaperones, acts as both an Hsp70 nucleotide-exchange factor and an inhibitor of the Hsp70-binding E3 ubiquitin ligase CHIP (carboxyl-terminus of Hsp70-interacting protein). The amino-terminal domain of Bag2 (Bag2-NTD), which is required for inhibition of CHIP, has no sequence homologs in the PDB. Native and selenomethionyl (SeMet) forms of Bag2-NTD were crystallized by hanging-drop vapor diffusion. Native Bag2-NTD crystals diffracted to 2.27 Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 75.5, b = 84.7, c = 114.1 Å. SeMet Bag2-NTD crystals diffracted to 3.10 Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 37.2, b = 53.3, c = 86.7 Å. Phases for the SeMet Bag2-NTD crystal were solved by single-wavelength anomalous diffraction. Initial phasing and model building using the 3.10 Å resolution SeMet Bag2-NTD data set suggested that Bag2-NTD forms a dimer and adopts a fold distinct from those of any domains annotated in the Pfam or SMART domain databases.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"647-51"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370901/pdf/f-68-00647.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30678523","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 analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii. 鲍曼不动杆菌对羟基苯乙酸 3-羟化酶还原酶成分的结晶和初步 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: 2012-05-24 DOI: 10.1107/S1744309112016909

Worrapoj Oonanant, Jeerus Sucharitakul, Pimchai Chaiyen, Jirundon Yuvaniyama

{"title":"Crystallization and preliminary X-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii.","authors":"Worrapoj Oonanant, Jeerus Sucharitakul, Pimchai Chaiyen, Jirundon Yuvaniyama","doi":"10.1107/S1744309112016909","DOIUrl":"10.1107/S1744309112016909","url":null,"abstract":"p-Hydroxyphenylacetate 3-hydroxylase (HPAH) from Acinetobacter baumannii catalyzes the hydroxylation of p-hydroxyphenylacetate (HPA) at the ortho position to yield 3,4-dihydroxyphenylacetate (DHPA). HPAH from A. baumannii is a two-component flavoprotein consisting of a smaller reductase (C(1)) component and a larger oxygenase (C(2)) component. The C(1) component supplies a reduced flavin in its free form to the C(2) counterpart for hydroxylation. In addition, HPA can bind to C(1) and enhance the flavin-reduction rate without becoming hydroxylated. The recombinant C(1) component was purified and crystallized using the microbatch method at 295 K. X-ray diffraction data were collected to 2.3 Å resolution using synchrotron radiation on the BL13B1 beamline at NSRRC, Taiwan. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 47.78, b = 59.92, c = 211.85 Å, and contained two molecules of C(1) per asymmetric unit.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"720-3"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370920/pdf/f-68-00720.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30679349","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 analysis of the haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58. 农杆菌 C58 中卤代烃脱卤酶 DatA 的结晶和初步 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/S1744309112013942

Tomoko Mase, Hideya Yabuki, Masahiko Okai, Jun Ohtsuka, Fabiana Lica Imai, Yuji Nagata, Masaru Tanokura

{"title":"Crystallization and preliminary X-ray analysis of the haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58.","authors":"Tomoko Mase, Hideya Yabuki, Masahiko Okai, Jun Ohtsuka, Fabiana Lica Imai, Yuji Nagata, Masaru Tanokura","doi":"10.1107/S1744309112013942","DOIUrl":"10.1107/S1744309112013942","url":null,"abstract":"Haloalkane dehalogenases are enzymes that catalyze the hydrolytic reaction of a wide variety of haloalkyl substrates to form the corresponding alcohol and hydrogen halide products. DatA from Agrobacterium tumefaciens C58 is a haloalkane dehalogenase that has a unique pair of halide-binding residues, asparagine (Asn43) and tyrosine (Tyr109), instead of the asparagine and tryptophan that are conserved in other members of the subfamily. DatA was expressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method with a reservoir solution consisting of 0.1 M CHES pH 8.6, 1.0 M potassium sodium tartrate, 0.2 M lithium sulfate, 0.01 M barium chloride. X-ray diffraction data were collected to 1.70 Å resolution. The space group of the crystal was determined as the primitive tetragonal space group P422, with unit-cell parameters a = b = 123.7, c = 88.1 Å. The crystal contained two molecules in the asymmetric unit.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"652-4"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370902/pdf/f-68-00652.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30678522","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 analysis of the C-terminal domain of CCM2, part of a novel adaptor protein involved in cerebral cavernous malformations. 参与脑海绵畸形的新型适配蛋白 CCM2 的 C 端结构域的结晶和初步 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/S1744309112016181

Xiaoyan Wang, Jingjin Ding, Dacheng Wang

引用次数: 0

Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus. 烟曲霉udp -半乳糖酰脲酶的纯化、结晶及x射线衍射初步数据。

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/S1744309112017915

George A Penman, Deborah E A Lockhart, Andrew Ferenbach, Daan M F van Aalten

引用次数: 4

Crystallization and preliminary X-ray crystallographic analysis of bacterial tRNA(Sec) in complex with seryl-tRNA synthetase. 细菌 tRNA(Sec) 与丝氨酰-tRNA 合成酶复合物的结晶和初步 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/S1744309112016004

Yuzuru Itoh, Shun Ichi Sekine, Shigeyuki Yokoyama

引用次数: 0

Crystallization and preliminary X-ray diffraction of malate dehydrogenase from Plasmodium falciparum. 恶性疟原虫苹果酸脱氢酶的结晶和初步 X 射线衍射。

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/S1744309112014571

Carsten Wrenger, Ingrid B Müller, Sabine Butzloff, Rositsa Jordanova, Sergey Lunev, Matthew R Groves

{"title":"Crystallization and preliminary X-ray diffraction of malate dehydrogenase from Plasmodium falciparum.","authors":"Carsten Wrenger, Ingrid B Müller, Sabine Butzloff, Rositsa Jordanova, Sergey Lunev, Matthew R Groves","doi":"10.1107/S1744309112014571","DOIUrl":"10.1107/S1744309112014571","url":null,"abstract":"The expression, purification, crystallization and preliminary X-ray diffraction characterization of malate dehydrogenase (MDH) from the malarial parasite Plasmodium falciparum (PfMDH) are reported. In order to gain a deeper understanding of the function and role of PfMDH, the protein was purified to homogeneity. The purified protein crystallized in space group P1, with unit-cell parameters a = 72, b = 157, c = 159 Å, α = 105, β = 101, γ = 95°. The resulting crystals diffracted to a maximal resolution of 2.24 Å and the structure has been solved by molecular replacement, with 16 monomers in the asymmetric unit. The 16 monomers are arranged into four independent tetramers, in agreement with previous reports demonstrating the tetrameric solution state of PfMDH. The X-ray structure of PfMDH is expected to clarify the differences in catalysis by PfMDH compared with other MDH family members and to provide a basis for the structure-based design of specific PfMDH inhibitors as well as general MDH inhibitors.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":" ","pages":"659-62"},"PeriodicalIF":0.9,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370904/pdf/f-68-00659.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30681013","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 of the novel S-adenosyl-L-methionine-dependent C-methyltransferase CouO from Streptomyces rishiriensis and preliminary diffraction data analysis. 新型 S-腺苷-L-蛋氨酸依赖型 C-甲基转移酶 CouO 的结晶和初步衍射数据分析。

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/S1744309112017137

Andrzej Lyskowski, Martin Tengg, Georg Steinkellner, Helmut Schwab, Mandana Gruber-Khadjawi, Karl Gruber

引用次数: 0