Biological Crystallography

 

Acta Cryst. (2008). D64, 705-710  [ doi:10.1107/S0907444908010032 ]

Structural basis for the high-affinity binding of pyrrolotriazine inhibitors of p38 MAP kinase

J. S. Sack, K. F. Kish, M. Pokross, D. Xie, G. J. Duke, J. A. Tredup, S. E. Kiefer and J. A. Newitt

Synopsis: The crystal structures of p38 MAP kinase complexed with two pyrrolotriazine-based inhibitors led to the elucidation of the high-affinity binding mode of these compounds.

PDB references: 2rg6 and 3bv3

Online 18 June 2008

 

Acta Cryst. (2008). D64, 711-729  [ doi:10.1107/S0907444908010202 ]

Exploiting the anisotropy of anomalous scattering boosts the phasing power of SAD and MAD experiments

M. Schiltz and G. Bricogne

Synopsis: It is shown that the anisotropy of anomalous scattering (AAS) is a significant and ubiquitous effect in data sets collected at an absorption edge and that its exploitation can substantially enhance the phasing power of single- or multi-wavelength anomalous diffraction. The improvements in the phases are typically of the same order of magnitude as those obtained in a conventional approach by adding a second-wavelength data set to a SAD experiment.

Online 18 June 2008

 

Acta Cryst. (2008). D64, 730-737  [ doi:10.1107/S0907444908011323 ]

Structure and sugar-specificity of basic winged-bean lectin: structures of new disaccharide complexes and a comparative study with other known disaccharide complexes of the lectin

K. A. Kulkarni, S. Katiyar, A. Surolia, M. Vijayan and K. Suguna

Synopsis: Crystal structures of winged-bean basic agglutinin with disaccharides having glycosidic linkages that differ from those in the A and B blood-group substances reveal the structural basis for the higher specifity of the lectin for the blood-group antigens.

PDB references: 2zml, 2zmn and 2zmk

Online 18 June 2008

 

Acta Cryst. (2008). D64, 738-744  [ doi:10.1107/S0907444908011578 ]

A general method for phasing novel complex RNA crystal structures without heavy-atom derivatives

M. P. Robertson and W. G. Scott

Synopsis: Using idealized known RNA secondary-structural fragments, it is demonstrated that it is possible to solve novel complex RNA structures without resort to heavy-atom phasing methods.

Online 18 June 2008

 

Acta Cryst. (2008). D64, 745-753  [ doi:10.1107/S0907444908012262 ]

Structures of Mycobacterium tuberculosis folylpolyglutamate synthase complexed with ADP and AMPPCP

P. G. Young, C. A. Smith, P. Metcalf and E. N. Baker

Synopsis: Crystal structures of M. tuberculosis folylpolyglutamate synthetase complexed with two nucleotides have been determined at 2.0 and 2.3 Å resolution, revealing an active-site loop movement and associated changes that influence substrate binding.

PDB references: 2vos and 2vor

Online 18 June 2008

 

Acta Cryst. (2008). D64, 754-763  [ doi:10.1107/S090744490801278X ]

High-resolution structure of unbound human immunodeficiency virus 1 subtype C protease: implications of flap dynamics and drug resistance

R. M. Coman, A. H. Robbins, M. M. Goodenow, B. M. Dunn and R. McKenna

Synopsis: The high-resolution structure of HIV-1 subtype C protease contributes to the understanding of flap dynamics and drug resistance.

PDB reference: 2r8n

Online 18 June 2008

 

Acta Cryst. (2008). D64, 764-783  [ doi:10.1107/S0907444908012845 ]

On the determinants of amide backbone exchange in proteins: a neutron crystallographic comparative study

B. C. Bennett, A. S. Gardberg, M. D. Blair and C. G. Dealwis

Synopsis: Backbone amide hydrogen/deuterium-exchange patterns can be directly observed from neutron crystal structures. For all the types of analysis performed, it is concluded that protection from exchange is only strongly correlated to secondary structure and the depth of the amide N atom.

Online 18 June 2008

 

Acta Cryst. (2008). D64, 784-791  [ doi:10.1107/S0907444908013474 ]

Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid)

I. Pallarès, D. Fernández, M. Comellas-Bigler, J. Fernández-Recio, S. Ventura, F. X. Avilés, W. Bode and J. Vendrell

Synopsis: The three-dimensional structure of human pancreatic carboxypeptidase A1 reveals the mode of binding of a polymer with drug-protecting effects and is used to apply optimal docking-area analysis to characterize binding sites for multiprotein complexes.

PDB reference: 2v77

Online 18 June 2008

 

Acta Cryst. (2008). D64, 792-802  [ doi:10.1107/S0907444908013978 ]

Structure determination of an anti-HIV-1 Fab 447-52D-peptide complex from an epitaxially twinned data set

A. K. Dhillon, R. L. Stanfield, M. K. Gorny, C. Williams, S. Zolla-Pazner and I. A. Wilson

Synopsis: Separation of two individual lattices within an epitaxially twinned data set allowed the crystal structure of the V3-specific neutralizing antibody 447-52D in complex with a V3 peptide (UG1033) to be determined. The structure confirms that the neutralization breadth of Fab 447-52D is likely to be attributable to the extensive focus on main-chain hydrogen-bond interactions with the peptide that permit the recognition of a range of V3 sequences.

PDB reference: 3c2a

Online 18 June 2008

 

Acta Cryst. (2008). D64, 803-809  [ doi:10.1107/S090744490801411X ]

1.6 Å structure of an NAD⁺-dependent quinate dehydrogenase from Corynebacterium glutamicum

J. Schoepe, K. Niefind and D. Schomburg

Synopsis: The crystal structure of an NAD⁺-dependent quinate dehydrogenase from C. glutamicum has been solved. Enzymatic assays show that this enzyme belongs to a new functional class of bacterial shikimate/quinate dehydrogenases.

PDB reference: 2nlo

Online 18 June 2008

 

Acta Cryst. (2008). D64, 810-814  [ doi:10.1107/S0907444908015540 ]

Federated repositories of X-ray diffraction images

S. Androulakis, J. Schmidberger, M. A. Bate, R. DeGori, A. Beitz, C. Keong, B. Cameron, S. McGowan, C. J. Porter, A. Harrison, J. Hunter, J. L. Martin, B. Kobe, R. C. J. Dobson, M. W. Parker, J. C. Whisstock, J. Gray, A. Treloar, D. Groenewegen, N. Dickson and A. M. Buckle

Synopsis: A suite of deposition tools have been created that allow X-ray diffraction images to be deposited in an open-access repository. The approach takes advantage of federated institutional repositories and aims to facilitate the archiving and sharing of raw X-ray diffraction images from the protein crystallography community.

Online 18 June 2008