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Volume 68(Pt 1);  2012 January 1

Editorial

Howard Einspahr, Manfred S. Weiss

Editorial.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 1. Published online 2011 December 24. doi: 10.1107/S1744309111053759
PMCID:
PMC3253823

Structural Communications

Rodrigo Torres, Nicholas Chim, Banumathi Sankaran, Céline Pujol, James B. Bliska, Celia W. Goulding

Comparison of the 2.45 Å resolution crystal structure of homotrimeric RipC, a putative citrate lyase β subunit from Y. pestis, with structural homologs reveals conserved RipC residues that are implicated in CoA binding.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 2–7. Published online 2011 December 24. doi: 10.1107/S1744309111048056
PMCID:
PMC3253824
Oren Yaniv, Yehuda Halfon, Linda J. W. Shimon, Edward A. Bayer, Raphael Lamed, Felix Frolow

The crystal structure at 1.0 Å resolution of the cellulose-binding CBM3b from the major scaffoldin subunit ScaA of A. cellulolyticus is described.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 8–13. Published online 2011 December 24. doi: 10.1107/S174430911104807X
PMCID:
PMC3253825
Sakiko Suzuki, Hisaaki Yanai, Mayumi Kanagawa, Satoko Tamura, Yuzo Watanabe, Kyotaro Fuse, Seiki Baba, Gen-ichi Sampei, Gota Kawai

The structure of PurL from T. thermophilus HB8 in complex with an adenine nucleotide is reported at 2.35 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 14–19. Published online 2011 December 24. doi: 10.1107/S1744309111048184
PMCID:
PMC3253826

Crystallization Communications

Shugang Yao, Jianxun Qi, Jun Liu, Rong Chen, Xiaocheng Pan, Xiaoying Li, Feng Gao, Chun Xia

The equine MHC class I molecule was crystallized in complex with β2-microglobulin and a CTL epitope and X-ray diffraction data were collected to 2.3 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 20–23. Published online 2011 December 24. doi: 10.1107/S1744309111038139
PMCID:
PMC3253827
Elfriede Dall, Hans Brandstetter

The enzymatic activation of human legumain requires both proteolytic cleavage and conformational reordering and is modulated by its substrate as well as cofactors. These biochemical findings are aided by the crystallization and initial crystallographic analysis of legumain.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 24–31. Published online 2011 December 24. doi: 10.1107/S1744309111048020
PMCID:
PMC3253828
Nazia Nasir, Rajan Vyas, Chetna Chugh, Mohammad Syed Ahangar, Bichitra K. Biswal

HisC2 from M. tuberculosis was cloned, overexpressed, purified and crystallized and the crystals were characterized.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 32–36. Published online 2011 December 24. doi: 10.1107/S1744309111045386
PMCID:
PMC3253829
Hideaki Ogata, Markus Knipp

The crystallization of recombinant nitrophorin 7 originating from the bloodsucking insect R. prolixus is described. The crystals diffracted to 1.8 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 37–40. Published online 2011 December 24. doi: 10.1107/S1744309111044708
PMCID:
PMC3253830
Zhiguang Ping, Yi Shi, Yanling Sun, Liping Ma, Ming Wang

Chicken interferon-γ receptor α chain was crystallized and diffraction data were collected to 2.0 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 41–44. Published online 2011 December 24. doi: 10.1107/S1744309111046318
PMCID:
PMC3253831
Elisabeth M. Meulenbroek, Navraj S. Pannu

Human Cockayne syndrome protein A has been cocrystallized with human DNA damage-binding protein 1 and data have been collected to 2.9 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 45–48. Published online 2011 December 24. doi: 10.1107/S1744309111045842
PMCID:
PMC3253832
Nobuo Okazaki, Motoyasu Adachi, Taro Tamada, Kazuo Kurihara, Takushi Ooga, Nobuo Kamiya, Seiki Kuramitsu, Ryota Kuroki

ADP-ribose pyrophosphatase-I, a Nudix enzyme, from T. thermophilus was crystallized for neutron diffraction. Neutron and X-ray diffraction data sets were collected to 2.1 and 1.5 Å resolution, respectively.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 49–52. Published online 2011 December 24. doi: 10.1107/S1744309111044551
PMCID:
PMC3253833
S. J. Tomanicek, A. Johs, M. S. Sawhney, L. Shi, L. Liang

The purification and crystallization of the outer membrane decaheme c-type cytochrome OmcA from S. oneidensis MR-1 are reported. The plate-like crystals belonged to the monoclinic space group P21 and diffracted to 3.25 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 53–55. Published online 2011 December 24. doi: 10.1107/S1744309111046082
PMCID:
PMC3253834
Bo-Young Yoon, Li Jiao, Hyung Ryong Moon, Jaeho Cha, Nam-Chul Ha

CbsA from T. neapolitana has been crystallized. Native data were collected to 2.0 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 56–58. Published online 2011 December 24. doi: 10.1107/S1744309111047099
PMCID:
PMC3253835
Richard D. Bunker, Kerry M. Loomes, Edward N. Baker

A human enzyme, DHDPSL, which is homologous to bacterial pyruvate-dependent aldolases but of unknown function, has been expressed, purified and crystallized with the use of in situ proteolysis. The crystals diffracted to 2.0 Å resolution and were suitable for structure determination.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 59–62. Published online 2011 December 24. doi: 10.1107/S1744309111048068
PMCID:
PMC3253836
Yanfeng Zhang, Xiaoli Gao

Recombinant wild-type l-lactate dehydrogenase from B. subtilis (BsLDH) was cocrystallized with fructose 1,6-bisphosphate and NAD+ and the crystal diffracted to 2.38 Å resolution. The H171C mutant of BsLDH was also crystallized as the apoenzyme and in complex with NAD+ and the crystals diffracted to 2.20 and 2.49 Å, respectively. All crystals belonged to space group

...
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 63–65. Published online 2011 December 24. doi: 10.1107/S1744309111048111
PMCID:
PMC3253837
Andrew Njagi Mugo, Jun Kobayashi, Bunzo Mikami, Kouhei Ohnishi, Toshiharu Yagi

Recombinant pyridoxine 4-oxidase from M. loti MAFF303099 was crystallized and diffraction data were collected to 2.2 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 66–68. Published online 2011 December 24. doi: 10.1107/S1744309111048688
PMCID:
PMC3253838
Xiaoyue Chen, Xuanhao Xu, Yuna Sun, Jingwen Zhou, Yuanyuan Ma, Liming Yan, Zhiyong Lou

A. thaliana dynamin-related protein 1A GTPase domain fused with its GTPase effector domain was overexpressed, purified and crystallized in a hexagonal crystal form that diffracted to 3.6 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 69–72. Published online 2011 December 24. doi: 10.1107/S1744309111047634
PMCID:
PMC3253839
Kimihito Usui, Umeharu Ohto, Toshinari Ochi, Toshiyuki Shimizu, Yoshinori Satow

This study reports the expression, purification, crystallization and preliminary X-ray crystallographic analysis of human lysosomal β-d-galactosidase.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 73–77. Published online 2011 December 24. doi: 10.1107/S1744309111047920
PMCID:
PMC3253840
Ae Kyung Park, Jeong Hye Lee, Young Min Chi, Jin Ho Moon

An orthorhombic crystal of an enoyl-(acyl-carrier protein) reductase from V. fischeri was obtained and diffraction data were collected to 2.7 Å resolution.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 78–80. Published online 2011 December 24. doi: 10.1107/S1744309111049426
PMCID:
PMC3253841
Simone Pellegrino, Jens Radzimanowski, Sean McSweeney, Joanna Timmins

The head domain of the DNA-repair protein RecN from D. radiodurans, composed of the amino- and carboxy-terminal domains, was crystallized. X-ray diffraction data were collected to 3.0 Å resolution and the crystals belonged to space group P21.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 81–84. Published online 2011 December 24. doi: 10.1107/S1744309111048743
PMCID:
PMC3253842
Fung T. Lay, Grant D. Mills, Mark D. Hulett, Marc Kvansakul

NaD1 is a potent antifungal plant defensin. Here, the crystallization and preliminary X-ray crystallographic analysis of NaD1 are reported in order to obtain insight into the structural basis of its antifungal activity.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 85–88. Published online 2011 December 24. doi: 10.1107/S1744309111049530
PMCID:
PMC3253843
Naomi J. Logsdon, Christopher E. Allen, Kanagalaghatta R. Rajashankar, Mark R. Walter

The purification and crystallization of the IL-20–IL-20R1–IL-20R2 ternary complex is described. A low-temperature SAD data set was collected using synchrotron radiation, which showed that the crystals belonged to space group P41212 or its enantiomorph P43212 and contained one ternary complex in the asymmetric unit.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 89–92. Published online 2011 December 24. doi: 10.1107/S1744309111049529
PMCID:
PMC3253844
Juliana Barbosa Coitinho, Débora Maria Abrantes Costa, Samuel Leite Guimarães, Alfredo Miranda de Góes, Ronaldo Alves Pinto Nagem

NahF is a salicylaldehyde dehydrogenase that is involved in the naphthalene-degradation pathway, converting salicylaldehyde into salicylate. The subcloning, expression, purification and preliminary X-ray diffraction studies at 2.42 Å resolution of P. putida G7 NahF are reported.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 93–97. Published online 2011 December 24. doi: 10.1107/S174430911105038X
PMCID:
PMC3253845
Dong-Won Im, Tae-O Kim, Ha Yun Jung, Ji Eun Oh, Se Jin Lee, Yong-Seok Heo

The RNA polymerase domain of primase from S. mutans strain UA159 was cloned, overexpressed, purified and crystallized. X-ray diffraction data were collected to a resolution of 1.60 Å.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 98–100. Published online 2011 December 24. doi: 10.1107/S1744309111050391
PMCID:
PMC3253846
Kyung Hye Seo, Ningning Zhuang, Joon-Yung Cha, Daeyoung Son, Kon Ho Lee

A DJ-1 homologue protein from A. thaliana (AtDJ-1D) has been crystallized. Diffraction data were collected to 2.05 Å resolution for structure determination by the multiple-wavelength anomalous dispersion (MAD) method.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 101–104. Published online 2011 December 24. doi: 10.1107/S1744309111050597
PMCID:
PMC3253847

Laboratory Communications

Xiaodi Deng, W. Sean Davidson, Thomas B. Thompson

Apolipoprotein A-IV crystals consisted of a long unit-cell edge (540 Å) with a high mosaic spread, making them intractable for X-ray diffraction analysis. Extreme dehydration in 60% PEG 3350 was utilized as a post-crystallization treatment as well a screening method to significantly sharpen the mosaic spread and increase the overall resolution of diffraction.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 105–110. Published online 2011 December 24. doi: 10.1107/S1744309111048706
PMCID:
PMC3253848
Matthew J. Wheeler, Silvia Russi, Michael G. Bowler, Matthew W. Bowler

The equilibrium relative humidity values for a number of the most commonly used precipitants in macromolecular crystallization have been measured using a humidity-control device and compared with independent values where available. The results will simplify experiments using the device.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 January 1; 68(Pt 1): 111–114. Published online 2011 December 24. doi: 10.1107/S1744309111054029
PMCID:
PMC3253849

Articles from Acta Crystallographica Section F: Structural Biology and Crystallization Communications are provided here courtesy of International Union of Crystallography