Seasonal variation of vitamin B12, B12 analogs, and phytoplankton in a Long Island estuary

Dissolved vitamin B12 concentrations in the Peconic Bay estuary, Long Island, were determined over a seasonal period by assay with the diatom Thalassiosira pseudonana clone 3H…

Supraspinatus-to-Glenoid Contact Occurs During Standardized Overhead Reaching Motion

Background: Rotator cuff tears may result from repeated mechanical deformation of the cuff tendons, and internal impingement of the supraspinatus tendon against the glenoid is one such proposed mechanism of deformation. Purpose: To (1) describe the changing proximity of the supraspinatus tendon to the glenoid during a simulated overhead reaching task and (2) determine the relationship between scapular morphology and this proximity. Additionally, the patterns of supraspinatus-to-glenoid proximity were compared with previously described patterns of supraspinatus-to-coracoacromial arch proximity. Study Design: Descriptive laboratory study. Methods: Shoulder models were created from magnetic resonance images of 20 participants. Standardized kinematics were imposed on the models to simulate functional reaching, and the minimum distances between the supraspinatus tendon and the glenoid and the supraspinatus footprint and the glenoid were calculated every 5° between 0° and 150° of humerothoracic elevation. The angle at which contact between the supraspinatus and the glenoid occurred was documented. Additionally, the relationship between glenoid morphology (version and inclination) and the contact angle was evaluated. Descriptive statistics were calculated for the minimum distances, and glenoid morphology was assessed using Pearson correlation coefficients and simple linear regressions. Results: The minimum distances between the tendon and the glenoid and between the footprint and the glenoid decreased as elevation increased. Contact between the tendon and the glenoid occurred in all participant models at a mean elevation of 123° ± 10°. Contact between the footprint and the glenoid occurred in 13 of 20 models at a mean of 139° ± 10°. Less glenoid retroversion was associated with lower tendon-to-glenoid contact angles (r = -0.76; R (2) = 0.58; P \u3c .01). Conclusion: This study found that the supraspinatus tendon progressively approximated the glenoid during simulated overhead reaching. Additionally, all participant models eventually made contact with the glenoid by 150° of humerothoracic elevation, although anatomic factors influenced the precise angle at which contact occurred. Clinical Relevance: Contact between the supraspinatus and the glenoid may occur frequently within the range of elevation required for overhead activities. Therefore, internal impingement may be a prevalent mechanism for rotator cuff deformation that could contribute to cuff pathology

The plug-based nanovolume Microcapillary Protein Crystallization System (MPCS)

This is the published version. Copyright International Union of CrystallographyThe Microcapillary Protein Crystallization System (MPCS) embodies a new semi-automated plug-based crystallization technology which enables nanolitre-volume screening of crystallization conditions in a plasticware format that allows crystals to be easily removed for traditional cryoprotection and X-ray diffraction data collection. Protein crystals grown in these plastic devices can be directly subjected to in situ X-ray diffraction studies. The MPCS integrates the formulation of crystallization cocktails with the preparation of the crystallization experiments. Within microfluidic Teflon tubing or the microfluidic circuitry of a plastic CrystalCard, ~10-20 nl volume droplets are generated, each representing a microbatch-style crystallization experiment with a different chemical composition. The entire protein sample is utilized in crystallization experiments. Sparse-matrix screening and chemical gradient screening can be combined in one com­prehensive `hybrid' crystallization trial. The technology lends itself well to optimization by high-granularity gradient screening using optimization reagents such as precipitation agents, ligands or cryoprotectants

The plug-based nanovolume Microcapillary Protein Crystallization System (MPCS)

The Microcapillary Protein Crystallization System (MPCS) is a new protein-crystallization technology used to generate nanolitre-sized crystallization experiments for crystal screening and optimization. Using the MPCS, diffraction-ready crystals were grown in the plastic MPCS CrystalCard and were used to solve the structure of methionine-R-sulfoxide reductase

An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

An ensemble of crystal structures are reported for 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase from B. pseudomallei. The structures include two vanadate complexes, revealing the structure of a close analogue of the transition state for phosphate transfer

Nanovolume optimization of protein crystal growth using the microcapillary protein crystallization system

The Microcapillary Protein Crystallization System (MPCS) is used to successfully optimize protein crystals from 28 out of 29 tested proteins. Six protein structures have been determined from diffraction-ready crystals grown inside and harvested directly from the MPCS CrystalCards, which are compatible with the recently commercialized and automated MPCS Plug Maker instrument

Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus

Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of avian influenza A viruses to mammals. However, the recently emerged pandemic H1N1 viruses lack these amino acids. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of lysine at position 627 and confers efficient viral replication to pandemic H1N1 viruses in mammals. Moreover, a basic amino acid at position 591 of PB2 substantially increased the lethality of an avian H5N1 virus in mice. We also present the X-ray crystallographic structure of the C-terminus of a pandemic H1N1 virus PB2 protein. Arginine at position 591 fills the cleft found in H5N1 PB2 proteins in this area, resulting in differences in surface shape and charge for H1N1 PB2 proteins. These differences may affect the protein's interaction with viral and/or cellular factors, and hence its ability to support virus replication in mammals

Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening

The first crystal structure is reported of a glutaryl-CoA dehydrogenase in the apo state without flavin adenine dinucleotide cofactor bound. Additional structures with small molecules complexed in the catalytic active site were obtained by fragment-based screening