The problem of undercounting of citations that are published only in supplementary material is studied for the journals Nature, Science, Cell and the Proceedings of the National Academy of Sciences (USA).
The crystal structure of Hsp33 from S. cerevisiae was solved at 2.40 Å resolution. Structural comparison showed that Hsp33 has a very similar structure to Hsp31, except for some deviations in helices α2–α3 of the core domain.
The crystal structure of human PI3K p85β iSH2 domain has been determined to 3.3 Å resolution. Comparison with the published structure of the bovine p85β iSH2 domain bound to the influenza A virus nonstructural protein 1 indicates that little or no structural change occurs upon complex formation. Structural analysis of human and bovine p85β iSH2 domains reveals conformational plasticity in the interhelical turn region of the coiled-coil motif.
The novel esterase Rv0045c from M. tuberculosis was expressed and purified to homogeneity. The crystals of native and SeMet-labelled Rv0045c protein that were obtained diffracted to resolutions of 2.7 and 3.0 Å, respectively.
A recombinant multiple cofactor-dependent DNA ligase from S. zilligii has been purified and crystallized. X-ray diffraction data were collected to 2.9 Å resolution and the crystals belonged to space group P1.
The cloning, purification and crystallization of the E. coli lipoproteins BamC, BamD and BamE is reported. X-ray diffraction data at high resolution were obtained for each of the proteins or protein domains.
The receptor-binding domain of botulinum neurotoxin serotype D was expressed in E. coli using a codon-optimized cDNA. The highly purified protein crystallized in space group P212121, with unit-cell parameters a = 60.8, b = 89.7, c = 93.9 Å, and the crystals diffracted to 1.65 Å resolution.
Wzi is a membrane protein from E. coli thought to be involved in the attachment of capsular polysaccharides to the bacterial surface. This reports describes recombinant Wzi's purification, crystallization and the results of initial diffraction studies.
Information about the intermediate states in the oligomerization process of a pore-forming toxin is lacking. Two oligomerization-deficient mutants of aerolysin, a major virulence factor secreted by A. hydrophila, which is involved in gastrointestinal infections in humans, have been crystallized in their proteolyzed forms and their preliminary X-ray analysis is reported.
The coupling region NBD94674–781 of Py235 from P. yoelii was cloned, overexpressed, purified and crystallized. The crystals belonged to space group C2 and diffracted to 2.9 Å resolution using synchrotron radiation.
The preparation and successful crystallization of the Grb7 SH2 domain in complex with the specific cyclic peptide inhibitor G7-18NATE are reported. This structure is anticipated to reveal the basis of the binding affinity and specificity and to assist with the development of second-generation inhibitors of Grb7, which is involved in cancer progression.
Diffraction from crystals of the cobalamin methyltransferases CobJ, CobM, CobF and CobL (full-length and C-terminal domain) from R. capsulatus is reported; three of these enzymes also catalyse the auxiliary reactions of ring contraction (CobJ), decarboxylation (CobL) and deacylation (CobF).
The ferritin homolog, BfrB (Rv3841), from Mycobacterium tuberculosis has been purified, crystallized, and diffraction data were collected to 2.5 Å resolution. Here, preliminary crystallographic characterization and SAXS analyses are reported.
The C-terminal fragment of Streptococcus agalactiae (group B streptococcus) major (backbone) pilin GBS80 was purified and crystallized in two different space groups. Single-wavelength anomalous dispersion (SAD) data collected to 2.0 Å resolution on a iodide (NaI) derivative crystal using the home source were used to obtain initial phases.
Nattokinase, a protein found in high levels in the traditional Japanese food natto, has been reported to have high thrombolytic activity. In the present study, the crystallization of native nattokinase and the collection of X-ray diffraction date from a nattokinase crystal to a resolution of 1.74 Å are reported.
NADPH-dependent 5-keto-D-gluconate reductase from G. suboxydans IFO12528 (5KGR) was expressed, purified and crystallized with 5-keto-D-gluconate and NADPH using the sitting-drop vapour-diffusion method. Crystals of the 5KGR–NADPH complex and of the 5KGR–NADPH–5-keto-D-gluconate complex diffracted X-rays to 1.75 and 2.26 Å resolution, respectively.