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This journal provides early access to some articles.
Volume 65(Pt 9);  September 1, 2009
Structural Communications
Guennadi Kozlov, Long Nguyen, Jessica Pearsall, Kalle Gehring
Here, the crystal structure of adenylosuccinate lyase from Escherichia coli was determined to 1.9 Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 857–861. Published online Aug 20, 2009. doi: 10.1107/S1744309109029674
PMCID:
PMC2795585
Anna Brzuszkiewicz, Elżbieta Nowak, Zbigniew Dauter, Mirosława Dauter, Hubert Cieśliński, Anna Długołęcka, Józef Kur
The crystal structure of the esterase EstA from a cold-adapted bacterium was determined in a form that was covalently inhibited by monoethylphosphonate.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 862–865. Published online Aug 20, 2009. doi: 10.1107/S1744309109030826
PMCID:
PMC2795586
Jelena Zaitseva, Kathleen M. Meneely, Audrey L. Lamb
The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 866–869. Published online Aug 20, 2009. doi: 10.1107/S1744309109032217
PMCID:
PMC2795587
Crystallization Communications
Yumiko Mishima, Franck Coste, Vanessa Bobezeau, Nadège Hervouet, Christine Kellenberger, Alain Roussel
Crystals of the N-terminal domain of Gram-negative bacteria-binding protein 3 of D. melanogaster grown from PEG solutions are monoclinic (space group C2) and diffract to 1.7 Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 870–873. Published online Aug 20, 2009. doi: 10.1107/S1744309109014997
PMCID:
PMC2795588
Yuichiro Kezuka, Yasuo Yoshida, Takamasa Nonaka
The βC-S lyases from two oral bacteria, Streptococcus anginosus and S. gordonii, were cloned, overproduced, purified and crystallized. The obtained crystals were characterized by X-ray diffraction.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 874–877. Published online Aug 20, 2009. doi: 10.1107/S1744309109030371
PMCID:
PMC2795589
Hideaki Ogata, Patrick Stolle, Matthias Stehr, Georg Auling, Wolfgang Lubitz
The crystallization of the metallo-cofactor (R2F) of native ribonucleotide reductase isolated from the Mn-requiring Gram-positive bacterium C. ammoniagenes is described. The crystals diffracted to 1.36 Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 878–880. Published online Aug 20, 2009. doi: 10.1107/S1744309109028978
PMCID:
PMC2795590
Charlotte Förster, Dominik Oberthuer, Jiang Gao, André Eichert, Frederick G. Quast, Christian Betzel, Andreas Nitsche, Volker A. Erdmann, Jens P. Fürste
An all-LNA duplex was designed from the stem region of an RNA aptamer which has been generated against ricin. The LNA duplex was crystallized and preliminary X-ray diffraction analysis revealed diffraction to a resolution of up to 2.8 Å.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 881–885. Published online Aug 22, 2009. doi: 10.1107/S1744309109029145
PMCID:
PMC2795591
Sayoko Matsuda, Nana Yokochi, Yu Yoshikane, Jun Kobayashi, Chu Nhat Huy, Seiki Baba, Seiki Kuramitsu, Bunzo Mikami, Toshiharu Yagi
Recombinant 4-pyridoxolactonase from M. loti MAFF303099 was crystallized in two forms and diffraction data were collected to 2.0 and 1.9 Å resolution, respectively.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 886–889. Published online Aug 22, 2009. doi: 10.1107/S1744309109028772
PMCID:
PMC2795592
Lindsay A. Matthews, Andrew Duong, Ajai A. Prasad, Bernard P. Duncker, Alba Guarné
To understand the role of the Cdc7–Dbf4 complex in checkpoint responses, a fragment of Saccharomyces cerevisiae Dbf4 encom­passing motif N was isolated, overproduced and crystallized.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 890–894. Published online Aug 22, 2009. doi: 10.1107/S1744309109029376
PMCID:
PMC2795593
Mads Gabrielsen, Alan Riboldi-Tunnicliffe, Puteri Shafinaz Abdul-Rahman, Emida Mohamed, Wan Izlina Wan Ibrahim, Onn Haji Hashim, Neil W. Isaacs, Richard J. Cogdell
Galactose-binding lectin from champedak was crystallized at 293 K. Preliminary X-ray diffraction analyses are reported.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 895–897. Published online Aug 22, 2009. doi: 10.1107/S1744309109029303
PMCID:
PMC2795594
S. D. Streeter, J. E. McGeehan, G. G. Kneale
The crystallization of a novel controller protein is reported and its interaction with DNA is characterized.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 898–901. Published online Aug 22, 2009. doi: 10.1107/S1744309109028681
PMCID:
PMC2795595
Fabio Marcio Squina, Rolf Alexander Prade, Hongliang Wang, Mario Tyago Murakami
The crystallization and preliminary X-ray diffraction studies of an endo-1,5-α-arabinanase from hyperthermophilic T. petrophila are reported. The crystals diffracted to 2.86 Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 902–905. Published online Aug 22, 2009. doi: 10.1107/S1744309109029844
PMCID:
PMC2795596
Miranda L. Byrne-Steele, Joseph D. Ng
The proliferating cell nuclear antigen (PCNA) from a novel hyperthermophilic archaeon Thermococcus thioreducens has been crystallized, and diffraction data have been collected to 1.86 Å.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 906–909. Published online Aug 22, 2009. doi: 10.1107/S174430910903036X
PMCID:
PMC2795597
Katherine H. Sippel, Susan K. Boehlein, Yoshihisa Sakai, Jeanne G. Quirit, Mavis Agbandje-McKenna, Charles J. Rosser, Robert McKenna
Single orthorhombic crystals of M. genitalium protein MG289 have been grown and shown to diffract X-rays to 2.8 Å resolution with good statistics. The structure obtained from these data will help to provide insight into the function of the protein as well as improving the understanding of its role in this human pathogen.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 910–912. Published online Aug 22, 2009. doi: 10.1107/S1744309109030565
PMCID:
PMC2795598
Zui Fujimoto, Isao Shiga, Yoshifumi Itoh, Keitarou Kimura
Poly-γ-glutamate hydrolase from bacteriophage ΦNIT1 was crystallized by the sitting-drop vapour-diffusion method and the crystals diffracted to beyond 2.4 Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 913–916. Published online Aug 22, 2009. doi: 10.1107/S1744309109029881
PMCID:
PMC2795599
Kayzad S. Nilgiriwala, Subhash C. Bihani, Amit Das, Vishal Prashar, Mukesh Kumar, Jean-Luc Ferrer, Shree Kumar Apte, M. V. Hosur
A new alkaline phosphatase enzyme from Sphingomonas sp. strain BSAR-1, termed PhoK, has been shown to be useful in uranium bioprecipitation. PhoK has been expressed, purified and crystallized.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 917–919. Published online Aug 22, 2009. doi: 10.1107/S1744309109031133
PMCID:
PMC2795600
Marta Marques, Ricardo Coelho, Inês A. C. Pereira, Pedro M. Matias
Crystals of the soluble form of the [NiFeSe] hydrogenase from D. vulgaris Hildenborough were obtained and belonged to the monoclinic space group P21, with unit-cell parameters a = 60.57, b = 91.05, c = 66.85 Å, β = 101.46°.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 920–922. Published online Aug 22, 2009. doi: 10.1107/S1744309109031261
PMCID:
PMC2795601
Tomoko Mase, Keiko Kubota, Ken-ichi Miyazono, Yutaka Kawarabayasi, Masaru Tanokura
Flap endonuclease 1 from D. amylolyticus was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 2.00 Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 923–925. Published online Aug 22, 2009. doi: 10.1107/S1744309109031248
PMCID:
PMC2795602
A. V. Kladova, O. Yu. Gavel, A. Mukhopaadhyay, D. R. Boer, S. Teixeira, V. L. Shnyrov, I. Moura, J. J. G. Moura, M. J. Romão, J. Trincão, S. A. Bursakov
Adenylate kinase (AK) from D. gigas was purified and crystallized in three different metal-bound forms: Zn2+–AK, Co2+–AK and Fe2+–AK.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 926–929. Published online Aug 22, 2009. doi: 10.1107/S1744309109029157
PMCID:
PMC2795603
Yu Wai Chen, Toshitaka Tajima, Martin Rees, Mitla Garcia-Maya
The ubiquitin-like domain of human hHR23A protein was crystallized by the hanging-drop vapour-diffusion method in space group P6522 and diffraction data were collected to 1.97 Å resolution. Structure solution by molecular replacement is described.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 930–932. Published online Aug 26, 2009. doi: 10.1107/S1744309109031376
PMCID:
PMC2795604
Kazuaki Matoba, Takeshi Nara, Takashi Aoki, Teruki Honma, Akiko Tanaka, Masayuki Inoue, Shigeru Matsuoka, Daniel Ken Inaoka, Kiyoshi Kita, Shigeharu Harada
Aspartate transcarbamoylase, the second enzyme of the de novo pyrimidine-biosynthetic pathway, from T. cruzi has been purified and crystallized for X-ray structure analysis.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 933–936. Published online Aug 26, 2009. doi: 10.1107/S1744309109031959
PMCID:
PMC2795605
Somnath Mukherjee, Samita Maity, Sobhan Roy, Suvankar Ghorai, Mrinmay Chakrabarti, Rachit Agarwal, Debajyoti Dutta, Ananta Kumar Ghosh, Amit Kumar Das
The cloning, overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of glyceraldehyde-3-phosphate dehydrogenase from A. mylitta are reported.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 937–940. Published online Aug 26, 2009. doi: 10.1107/S174430910903214X
PMCID:
PMC2795606
Arihiro Osanai, Shigeharu Harada, Kimitoshi Sakamoto, Hironari Shimizu, Daniel Ken Inaoka, Kiyoshi Kita
Rhodoquinol-fumarate reductase is a key enzyme in the anaerobic respiratory chain of adult A. suum mitochondria. Its crystallization in the presence of a mixture of octaethyleneglycol monododecyl ether and n-dodecyl-β-d-maltopyranoside in a form suitable for X-ray structure analysis is reported.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 941–944. Published online Aug 26, 2009. doi: 10.1107/S1744309109031352
PMCID:
PMC2795607
Janet Newman, Edward H. Cohen, Leah Cosgrove, Kris Kopacz, Daniel T. Dransfield, Timothy E. Adams, Thomas S. Peat
Complexes of both hIGF-II and hIGF-IIE with a Fab have been crystallized and investigated by X-ray analysis.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 945–948. Published online Aug 26, 2009. doi: 10.1107/S1744309109024932
PMCID:
PMC2795608
Anuradha Balasubramanian, Karthe Ponnuraj
Jack bean urease was purified and crystallized and X-ray diffraction data were collected to 2.05 Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 949–951. Published online Aug 26, 2009. doi: 10.1107/S1744309109031662
PMCID:
PMC2795609
Kim-Hung Huynh, Sampath Natarajan, Jeongyoon Choi, Na-Hyun Song, Jeong-Gu Kim, Byoung-Moo Lee, Yeh-Jin Ahn, Lin-Woo Kang
Leucine aminopeptidase, an exopeptidase that hydrolyzes leucine from the N-terminus of polypeptides, from X. oryzae pv. oryzae was cloned, expressed and crystallized.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 952–955. Published online Aug 26, 2009. doi: 10.1107/S1744309109031467
PMCID:
PMC2795610
Denis Kudlinzki, Christian Nagel, Ralf Ficner
The cloning, purification and crystallization of the C-terminal domain of human hPrp22 are reported. This communication also contains data for the preliminary X-ray diffraction analysis.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 956–958. Published online Aug 26, 2009. doi: 10.1107/S1744309109031844
PMCID:
PMC2795611
Hiroshi Hashimoto, Shigeta Kawaguchi, Kodai Hara, Keishi Nakamura, Toshiyuki Shimizu, Yutaka Tamaru, Mamoru Sato
Crystallization of Nanos.
Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2009; 65(Pt 9): 959–961. Published online Aug 26, 2009. doi: 10.1107/S1744309109032163
PMCID:
PMC2795612
Articles from Acta Crystallographica Section F: Structural Biology and Crystallization Communications are provided here courtesy of
International Union of Crystallography