Structural Biology and Crystallization Communications

Acta Cryst. (2009). F65, 654-659  [ doi:10.1107/S1744309109019605 ]

The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain

A. R. Conlan, M. L. Paddock, H. L. Axelrod, A. E. Cohen, E. C. Abresch, S. Wiley, M. Roy, R. Nechushtai and P. A. Jennings

Synopsis: The crystal structure of the anti-diabetic drug target mitoNEET obtained from a GFP fusion construct (1.4 Å resolution, R factor = 20.2%) shows that the CDGSH 2Fe-2S binding domains are superimposable with previously determined non-fused constructs. However, there is considerable flexibility in the position of the outer mitochondrial tethering arms resulting in two different conformations in the crystal structure.

PDB reference: 3ew0

Online 27 June 2009

Acta Cryst. (2009). F65, 660-664  [ doi:10.1107/S1744309109019654 ]

Interaction of an echinomycin-DNA complex with manganese ions

R. Pfoh, J. A. Cuesta-Seijo and G. M. Sheldrick

Synopsis: In the presence of Mn²⁺, a new crystal form of an echinomycin-d(ACGTACGT) complex is found which shows mixed base pairing next to the bis-intercalation site.

PDB reference: 3go3

Online 27 June 2009

Acta Cryst. (2009). F65, 665-670  [ doi:10.1107/S1744309109020302 ]

Structure of the lamin A/C R482W mutant responsible for dominant familial partial lipodystrophy (FPLD)

E. Magracheva, S. Kozlov, C. L. Stewart, A. Wlodawer and A. Zdanov

Synopsis: The crystal structure of the R482W mutant of the C-terminal domain of lamin A/C, which is responsible for familial partial lipodystrophy, has been determined at 1.5 Å resolution. A completely novel aggregation state of the mutated protein may be responsible for the changes in biological activity.

PDB reference: 3gef

Online 27 June 2009

Acta Cryst. (2009). F65, 671-677  [ doi:10.1107/S1744309109021423 ]

Inhibitor design for ribonuclease A: the binding of two 5'-phosphate uridine analogues

V. G. Tsirkone, K. Dossi, C. Drakou, S. E. Zographos, M. Kontou and D. D. Leonidas

Synopsis: The structure of ribonuclease A in complex with uridine 5'-phosphate and uridine 5'-diphosphate has been determined at 1.4 Å resolution in order to facilitate the rational design of selective and potent inhibitors.

PDB references: 3dxg and 3dxh

Online 27 June 2009

Acta Cryst. (2009). F65, 678-680  [ doi:10.1107/S1744309109018636 ]

Crystallization and preliminary crystallographic analysis of bifunctional -glutamylcysteine synthetase-glutatione synthetase from Streptococcus agalactiae

Y. Nakashima, H. Nii, B. E. Janowiak, O. W. Griffith and T. Hibi

Synopsis: The S. agalactiae bifunctional ligase for glutathione synthesis has been crystallized. Native data were collected to 2.8 Å resolution.

Online 27 June 2009

Acta Cryst. (2009). F65, 681-683  [ doi:10.1107/S1744309109019009 ]

Purification, crystallization and preliminary X-ray analysis of haemoglobin from ostrich (Struthio camelus)

S. S. Sundaresan, P. Ramesh, K. Sivakumar and M. N. Ponnuswamy

Synopsis: Purification, crystallization and preliminary X-ray analysis of haemoglobin from ostrich (Struthio camelus) has been carried out under 293 K temperature conditions. The ostrich is a large flightless bird which contains inositol tetrakisphosphate in erythrocytes and its whole blood oxygen affinity is higher. Efforts have been made to explore the structure-function relationship of ostrich heamoglobin.

Online 27 June 2009

Acta Cryst. (2009). F65, 684-687  [ doi:10.1107/S1744309109019216 ]

Purification, crystallization and preliminary X-ray diffraction analysis of the FeoB G domain from Methanococcus jannaschii

S. Köster, W. Kühlbrandt and Ö. Yildiz

Synopsis: The N-terminal domain of FeoB from Methanococcus jannaschii was overproduced, purified to homogeneity and crystallized in the presence of GTP and magnesium.

Online 27 June 2009

Acta Cryst. (2009). F65, 688-691  [ doi:10.1107/S1744309109019514 ]

Crystallization and preliminary X-ray diffraction studies of the tetramerization domain derived from the human potassium channel Kv1.3

A. Winklmeier, M. Weyand, C. Schreier, H. R. Kalbitzer and W. Kremer

Synopsis: The tetramerization domain of human Kv1.3 was cloned, expressed, purified and crystallized. The crystals belonged to space group I4 and diffracted to 1.2 Å resolution using synchrotron radiation.

Online 27 June 2009

Acta Cryst. (2009). F65, 692-694  [ doi:10.1107/S1744309109020107 ]

Crystallization and preliminary crystallographic studies of the single-chain variable fragment of antibody chA21 in complex with an N-terminal fragment of ErbB2

Y. Liu, H. Zhou, J. Zhu, Y. Gao, L. Niu, J. Liu and M. Teng

Synopsis: An antibody-antigen complex consisting of a single-chain variable fragment of the potential therapeutic antibody chA21 and an N-terminal fragment (residues 1-192) of the human ErbB2 extracellular domain was expressed, purified and crystallized. X-ray diffraction data were collected to 2.45 Å resolution.

Online 27 June 2009

Acta Cryst. (2009). F65, 695-697  [ doi:10.1107/S1744309109020132 ]

Crystallization and preliminary X-ray diffraction studies of AsaP1_E294A and AsaP1_E294Q, two inactive mutants of the toxic zinc metallopeptidase AsaP1 from Aeromonas salmonicida subsp. achromogenes

X. Bogdanovic, R. K. Singh, J. Hentschke, B. K. Gudmundsdóttir and W. Hinrichs

Synopsis: Crystallization and preliminary X-ray diffraction studies of AsaP1_E294A and AsaP1_E294Q, two inactive mutants of the toxic zinc metallopeptidase AsaP1 from A. salmonicida subsp. achromogenes, are reported.

Online 27 June 2009

Acta Cryst. (2009). F65, 698-701  [ doi:10.1107/S1744309109020296 ]

Crystallization and preliminary X-ray characterization of a glycerol dehydrogenase from the human pathogen Salmonella enterica serovar Typhimurium

A. T. Gonçalves, D. Marçal, M. A. Carrondo and F. J. Enguita

Synopsis: The expression, purification and crystallization of a glycerol dehydrogenase from S. typhimurium is decribed. The crystals diffracted to 3.5 Å resolution.

Online 27 June 2009

Acta Cryst. (2009). F65, 702-704  [ doi:10.1107/S1744309109020454 ]

Expression, purification, crystallization and preliminary X-ray studies of Vibrio cholerae pseudopilin EpsH

K. Raghunathan, F. S. Vago, T. Ball, N. Yakubova, D. Grindem, W. J. Wedemeyer and D. N. Arvidson

Synopsis: Recombinant V. cholerae EpsH has been expressed, purified and crystallized. The crystals diffracted to 1.71 Å resolution.

Online 27 June 2009

Acta Cryst. (2009). F65, 705-708  [ doi:10.1107/S1744309109020685 ]

Production, purification, crystallization and preliminary X-ray diffraction analysis of the HIV-2-neutralizing V3 loop-specific Fab fragment 7C8

H. Uchtenhagen, S. Sourial, R. Friemann, M. Ehnlund, A.-L. Spetz, R. A. Harris, C. Madhurantakam and A. Achour

Synopsis: Neutralizing Fab fragments of the HIV-2-binding murine antibody 7C8 were generated after purification from hybridoma cell-culture supernatant. Crystallization conditions were determined and diffraction data were collected to 2.7 Å resolution.

Online 27 June 2009

Acta Cryst. (2009). F65, 709-711  [ doi:10.1107/S1744309109020703 ]

Protein preparation, crystallization and preliminary crystallographic studies of Bacillus subtilis glycinamide ribonucleotide transformylase

Y.-H. Liang, X.-Y. Liu, J. Wang and L.-F. Li

Synopsis: In order to study the structure and function of B. subtilis glycinamide ribonucleotide transformylase, the purN gene was amplified, cloned into an expression vector and expressed in soluble form in Escherichia coli. The protein was purified to homogeneity and crystals suitable for X-ray data collection were obtained.

Online 27 June 2009

Acta Cryst. (2009). F65, 712-714  [ doi:10.1107/S1744309109021046 ]

A crystallizable form of the Streptococcus gordonii surface antigen SspB C-domain obtained by limited proteolysis

N. Forsgren, R. J. Lamont and K. Persson

Synopsis: The C-terminal domain of the S. gordonii surface protein SspB has been expressed, purified and crystallized. Diffraction data have been collected to 2.1 Å resolution.

Online 27 June 2009

Acta Cryst. (2009). F65, 715-718  [ doi:10.1107/S1744309109021460 ]

Production, purification and preliminary X-ray crystallographic studies of adeno-associated virus serotype 9

M. Mitchell, H.-J. Nam, A. Carter, A. McCall, C. Rence, A. Bennett, B. Gurda, R. McKenna, M. Porter, Y. Sakai, B. J. Byrne, N. Muzyczka, G. Aslanidi, S. Zolotukhin and M. Agbandje-McKenna

Synopsis: The purification, crystallization and preliminary X-ray crystallographic analyses of the AAV9 viral capsid are reported.

Online 27 June 2009

Acta Cryst. (2009). F65, 719-722  [ doi:10.1107/S1744309109022696 ]

Preliminary crystallographic studies of the regulatory domain of response regulator YycF from an essential two-component signal transduction system

H. Zhao, A. Heroux, R. D. Sequeira and L. Tang

Synopsis: The regulatory domain of response regulator YycF from an essential two-component signal transduction system has been crystallized and X-ray data have been collected at 1.95 Å resolution.

Online 27 June 2009

Acta Cryst. (2009). F65, 723-726  [ doi:10.1107/S174430910902291X ]

Preliminary structural characterization of human SOUL, a haem-binding protein

F. Freire, M. J. Romão, A. L. Macedo, S. S. Aveiro, B. J. Goodfellow and A. L. Carvalho

Synopsis: This manuscript describes the overexpression, purification and crystallization of human SOUL protein (hSOUL). hSOUL is a 23 kDa haem-binding protein that was first identified as the PP23 protein isolated from human full-term placenta.

Online 27 June 2009

Acta Cryst. (2009). F65, 727-729  [ doi:10.1107/S1744309109023082 ]

Crystallization and preliminary X-ray crystallographic studies of DesR, a thermosensing response regulator in a two-component signalling system from Streptococcus pneumoniae

A. K. Park, S. M. Bong, J. H. Moon and Y. M. Chi

Synopsis: The response regulator DesR from S. pneumoniae was cloned, expressed, purified and crystallized. A complete data set was collected to 1.7 Å resolution.

Online 27 June 2009

Acta Cryst. (2009). F65, 730-732  [ doi:10.1107/S1744309109023392 ]

Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) from Desulfovibrio gigas

S. Najmudin, C. Bonifácio, A. G. Duarte, S. R. Pualeta, I. Moura, J. J. G. Moura and M. J. Romão

Synopsis: Diifraction data have been collected for the apo form of the orange protein from D. gigas to 2.25 Å resolution in-house and to beyond 2.0 Å resolution at ESRF, Grenoble. The crystals belonged to a trigonal space group, with unit-cell parameters a = 43, b = 43, c = 106 Å.

Online 30 June 2009

Acta Cryst. (2009). F65, 733-735  [ doi:10.1107/S1744309109023409 ]

Crystallization and initial crystallographic analysis of phosphoglucosamine mutase from Bacillus anthracis

R. Mehra-Chaudhary, C. E. Neace and L. J. Beamer

Synopsis: The enzyme phosphoglucosamine mutase from B. anthracis participates in the peptidoglycan-biosynthetic pathway. The expression, purification and crystallization of this enzyme are described; diffraction data have been collected to 2.7 Å resolution.

Online 30 June 2009

Acta Cryst. (2009). F65, 736-738  [ doi:10.1107/S1744309109023495 ]

Purification, crystallization and preliminary crystallographic studies of a Kunitz-type proteinase inhibitor from tamarind (Tamarindus indica) seeds

D. N. Patil, Preeti, A. Chaudhry, A. K. Sharma, S. Tomar and P. Kumar

Synopsis: A 21 kDa Kunitz-type proteinase inhibitor was purified from tamarind (T. indica) seeds, crystallized and characterized by X-ray diffraction.

Online 30 June 2009

Acta Cryst. (2009). F65, 739-742  [ doi:10.1107/S1744309109023410 ]

Production, crystallization and preliminary crystallographic analysis of an exosite-containing fragment of human von Willebrand factor-cleaving proteinase ADAMTS13

M. Akiyama, S. Takeda, K. Kokame, J. Takagi and T. Miyata

Synopsis: A fragment of the ADAMTS13 ancillary domains (ADAMTS13-DTCS) has been expressed, purified and crystallized and the crystals have been characterized by X-ray diffraction.

Online 30 June 2009

Acta Cryst. (2009). F65, 743-745  [ doi:10.1107/S1744309109019873 ]

Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CusB

Y. Xu, B.-Y. Yun, S.-H. Sim, K. Lee and N.-C. Ha

Synopsis: This article describes how CusB from E. coli was overexpressed and the recombinant protein purified using Ni-NTA affinity, Q anion-exchange and gel-filtration chromatography, and how the purified CusB protein was crystallized using the vapour-diffusion method.

Online 30 June 2009