Biological Crystallography

 

Acta Cryst. (2010). D66, 855-864  [ doi:10.1107/S0907444910019591 ]

Diffraction cartography: applying microbeams to macromolecular crystallography sample evaluation and data collection

M. W. Bowler, M. Guijarro, S. Petitdemange, I. Baker, O. Svensson, M. Burghammer, C. Mueller-Dieckmann, E. J. Gordon, D. Flot, S. M. McSweeney and G. A. Leonard

Synopsis: New tools for the evaluation of the diffraction characteristics of crystals of macromolecules are presented in the context of the ESRF Upgrade MASSIF beamlines.

Online 9 July 2010

 

Acta Cryst. (2010). D66, 865-873  [ doi:10.1107/S0907444910019554 ]

Structure of the N-terminal fragment of Escherichia coli Lon protease

M. Li, A. Gustchina, F. S. Rasulova, E. E. Melnikov, M. R. Maurizi, T. V. Rotanova, Z. Dauter and A. Wlodawer

Synopsis: The medium-resolution structure of the N-terminal fragment of E. coli Lon protease shows that this part of the enzyme consists of two compact domains and a very long -helix.

PDB reference: 3ljc

Online 9 July 2010

 

Acta Cryst. (2010). D66, 874-880  [ doi:10.1107/S0907444910019876 ]

The first crystal structure of a gramicidin complex with sodium: high-resolution study of a nonstoichiometric gramicidin D-NaI complex

A. Olczak, M. L. Glówka, M. Szczesio, J. Bojarska, Z. Wawrzak and W. L. Duax

Synopsis: The crystal structure of the nonstoichiometric complex of gramicidin D with NaI has been studied using synchrotron radiation at 100 K.

PDB reference: 3l8l

Online 9 July 2010

 

Acta Cryst. (2010). D66, 881-888  [ doi:10.1107/S0907444910020081 ]

Structure of Staphylococcus aureus adenylosuccinate lyase (PurB) and assessment of its potential as a target for structure-based inhibitor discovery

P. K. Fyfe, A. Dawson, M.-T. Hutchison, S. Cameron and W. N. Hunter

Synopsis: The 2.5 Å resolution structure of S. aureus adenylosuccinate lyase is reported and compared with those of orthologues to assess its potential as a template for early stage drug discovery. AMP and a putative assignment of oxalate, the latter an artefact possibly arising from an impurity in the PEG used for crystallization, occupy the active site.

PDB reference: 2x75

Online 9 July 2010

 

Acta Cryst. (2010). D66, 889-900  [ doi:10.1107/S0907444910020421 ]

Validation of crystallographic models containing TLS or other descriptions of anisotropy

F. Zucker, P. C. Champ and E. A. Merritt

Synopsis: Guidelines and specific tests for validating macromolecular crystal structures that include TLS models are introduced. Validation may used to troubleshoot problems during refinement, to confirm the internal consistency of the model as part of deposition into the Protein Data Bank or to assess the plausibility of interpretating the boundary between two TLS groups as indicating a hinge point between structural domains.

Online 9 July 2010

 

Acta Cryst. (2010). D66, 901-908  [ doi:10.1107/S0907444910020664 ]

Quantitive evaluation of macromolecular crystallization experiments using 1,8-ANS fluorescence

D. Watts, J. Müller-Dieckmann, G. Tsakanova, V. S. Lamzin and M. R. Groves

Synopsis: A novel approach is presented for the visualization of crystallization experiments using fluorescence from trace amounts of a nonspecific dye.

Online 10 July 2010

 

Acta Cryst. (2010). D66, 909-917  [ doi:10.1107/S0907444910025771 ]

Structural and functional analysis of Rv0554 from Mycobacterium tuberculosis: testing a putative role in menaquinone biosynthesis

J. M. Johnston, M. Jiang, Z. Guo and E. N. Baker

Synopsis: The crystal structure of Rv0554 from M. tuberculosis has been determined, revealing a dimeric protein with an /-hydrolase fold. Functional assays failed to support a proposed role in menaquinone biosynthesis.

PDB references: 3e3a and 3hss

Online 10 July 2010

 

Acta Cryst. (2010). D66, 918-926  [ doi:10.1107/S0907444910020810 ]

Structural basis of the histidine-mediated vitamin D receptor agonistic and antagonistic mechanisms of (23S)-25-dehydro-1-hydroxyvitamin D₃-26,23-lactone

S. Kakuda, S. Ishizuka, H. Eguchi, M. T. Mizwicki, A. W. Norman and M. Takimoto-Kamimura

Synopsis: The molecular mechanism of the VDR-antagonistic action of TEI-9647 is investigated.

PDB references: 3a2h, 3a2i and 3a2j

Online 10 July 2010

 

Acta Cryst. (2010). D66, 927-933  [ doi:10.1107/S0907444910026041 ]

Promoting crystallization of antibody-antigen complexes via microseed matrix screening

G. Obmolova, T. J. Malia, A. Teplyakov, R. Sweet and G. L. Gilliland

Synopsis: The application of microseed matrix screening to the crystallization of related antibodies in complex with IL-13 is described. Both self-seeding or cross-seeding helped promote nucleation and increase the hit rate.

Online 14 July 2010

 

Acta Cryst. (2010). D66, 934-944  [ doi:10.1107/S0907444910025710 ]

Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase

M. Salin, E. G. Kapetaniou, M. Vaismaa, M. Lajunen, M. G. Casteleijn, P. Neubauer, L. Salmon and R. K. Wierenga

Synopsis: Crystallographic binding studies of a monomeric variant of triosephosphate isomerase (A-TIM) with a modified more extended binding pocket between loop-7 and loop-8 are reported. Wild-type TIM exclusively catalyses the isomerization of the C3-sugar phosphates dihydroxyacetonephosphate and D-glyceraldehyde-3-phosphate. These crystallographic studies show that the new binding pocket of A-TIM can also bind analogues of C4-sugar phosphates and C5-sugar phosphates.

PDB references: 2x16, 2x1s, 2x1r, 2x2g, 2x1t and 2x1u

Online 14 July 2010

 

Acta Cryst. (2010). D66, 945-949  [ doi:10.1107/S0907444910025783 ]

Enhancing MAD F_A data for substructure determination

H. Xu

Synopsis: A new statistical and computational procedure, which merges multiple F_A estimates into an averaged data set, is used to further improve the quality of the estimated anomalous amplitudes for substructure determination.

Online 14 July 2010

 

Acta Cryst. (2010). D66, 950-952  [ doi:10.1107/S0907444910023723 ]

Emerging from pseudo-symmetry: the redetermination of human carbonic anhydrase II in monoclinic P2₁ with a doubled a axis

A. H. Robbins, J. F. Domsic, M. Agbandje-McKenna and R. McKenna

Synopsis: The structure of human carbonic anhydrase II in the monoclinic P2₁ space group with a doubled a axis from that of the usually observed unit cell has been re-determined and shown that the choice for how the four molecules in the unit cell are grouped (based on their coordinates) into pairs that represent a single asymmetric unit determines whether or not rotational disorder is observed/created during refinement.

PDB reference: 3mwo

Online 9 July 2010