BIOBOARD

2012 ◽  
Vol 16 (06) ◽  
pp. 5-13

INDIA – Zinc Treatment for Infections in Children. JAPAN – Japan Pharma Portfolio Finds Renewed Strength through Record Growth in 2012. JAPAN – Joint Development of a Novel Lyophilized Dual Chamber Prefillable Syringe System. JAPAN – A Genetic Alternative to Fertilizer. SINGAPORE – Made-in-Singapore H5N1 Bird Flu Diagnostic Kit - Detects All Known Strains of H5N1 Virus with a Single Test. THAILAND – KEEEN, Thai Bioremediation Product, Awarded Gold Medal for "Bioremediation Agent developed to Greenovation Product". EUROPE – MorphoSys Antibody Reaches Major Milestone in Collaboration with Roche. EUROPE – New Technique to Predict Heart Attacks. USA – FEI Launches 'Living Lab' for Structural Biology Research at NIH. USA – Synthetic Platelets Built to Treat Bleeding. USA – Software Scans Tongue for Signs of Disease. USA – US Legislation Will Ensure Tighter Checks on Foreign Drug Factories.

2019 ◽  
Vol 75 (a1) ◽  
pp. a120-a120
Author(s):  
Surajit Banerjee ◽  
Malcolm Capel ◽  
Igor Kourinov ◽  
Anthony Lynch ◽  
Frank Murphy ◽  
...  

2018 ◽  
Vol 114 (3) ◽  
pp. 524a
Author(s):  
Surajit Banerjee ◽  
Malcolm Capel ◽  
Igor Kourinov ◽  
Anthony Lynch ◽  
Frank Murphy ◽  
...  

Author(s):  
Scott Spearing ◽  
Sang Young Son ◽  
Jeffrey Allen ◽  
Lisa A. Monaco

A team from the structural biology group located at the Marshall Space Flight Center in Huntsville Alabama is developing a platform suitable for cross-disciplinary microchannel research. The original objective of this engineering development effort was to deliver a multi-user flight-certified facility for iterative investigations of protein crystal growth; that is, Iterative Biological Crystallization. However, the unique capabilities of this facility are not limited to the low-gravity structural biology research community. Microchannel-based research in a number of other areas may be greatly accelerated through use of this facility. In particular, the potential for gas-liquid flow investigations and cellular biological research utilizing the exceptional pressure control and simplified coupling to macroscale diagnostics inherent with the facility will be discussed. Also noted will be the opportunities for research-specific modifications to the microchannel configuration, control and diagnostics.


2011 ◽  
Vol 67 (a1) ◽  
pp. C482-C483 ◽  
Author(s):  
I. Kourinov ◽  
S. E. Ealick ◽  
M. Capel ◽  
S. Banerjee ◽  
F. Murphy ◽  
...  

2002 ◽  
Vol 10 (1) ◽  
pp. 43-45 ◽  
Author(s):  
J. J. Rehr ◽  
A. L. Ankudinov

There has been dramatic progress over the past decade both in theory and inab initiocalculations of X-ray absorption fine structure. Significant progress has also been made in understanding X-ray absorption near-edge structure (XANES). This contribution briefly reviews the developments in this field leading up to the current state. One of the key advances has been the development of severalab initiocodes such asFEFF, which permit an interpretation of the spectra in terms of geometrical and electronic properties of a material. Despite this progress, XANES calculations have remained challenging both to compute and to interpret. However, recent advances based on parallel Lanczos multiple-scattering algorithms have led to speed increases of typically two orders of magnitude, making fast calculations practicable. Improvements in the interpretation of near-edge structure have also been made. It is suggested that these developments can be advantageous in structural biology,e.g.in post-genomics studies of metalloproteins.


2014 ◽  
Vol 70 (a1) ◽  
pp. C19-C19
Author(s):  
Soichi Wakatsuki

X-ray free electron lasers (XFEL) have shown the promise of providing new opportunities in structural biology research with their extremely high peak brilliance and short pulses. It is reaching the stage where biologically important questions can be tackled using XFEL based on the "diffract-before-destroy" concept. The first part of this presentation will focus on macromolecular crystallography using XFEL with results obtained at LCLS so far and future scope. R&D efforts being pursued at SLAC/LCLS include new beam modes, (two-color beam for de novo phasing, wider bandwidth for SAXS/WAXS and spectroscopy), beam multiplexing, a dedicated new station for in-air data collection, next generation detectors, data analysis incorporating pulse-by-pulse spectrometer measurements and post refinement. These projects are being pursued in collaboration with many groups locally and globally with a goal to provide integrated facilities for cutting edge structural biology research. For example, two-color self-seeded XFEL mode is being developed for simultaneous recording of diffraction data at two energies in order to optimize the dispersive difference between the two wavelengths for phasing. Another area of collaborative effort is a development of dedicated station for in-air data collection with a variety of sample delivery schemes. The second part will discuss a possible roadmap towards atomic resolution single particle imaging using XFEL. Here, key questions are ·Can XFEL single particle 3D structural analysis at atomic resolution be done? ·What is the pulse characteristics required? ·Can we overcome the radiation damage at soft X-ray regime? ·What is the highest resolution attainable in comparison with cryoEM? A workshop at LCLS is being organized to discuss these questions in 4 areas: radiation damage, image reconstruction algorithm, beam modes and instrumentation, sample delivery and heterogeneity. The outcome of the workshop and follow-up discussions will be presented.


2014 ◽  
Vol 67 (12) ◽  
pp. 1732 ◽  
Author(s):  
Lyndel Mason ◽  
Parisa Amani ◽  
Megan Cross ◽  
Joshua Baker ◽  
Ulla-Maja Bailey ◽  
...  

New interventions against infectious diseases require a detailed knowledge and understanding of pathogen–host interactions and pathogeneses at the molecular level. The combination of the considerable advances in systems biology research with methods to explore the structural biology of molecules is poised to provide new insights into these areas. Importantly, exploring three-dimensional structures of proteins is central to understanding disease processes, and establishing structure–function relationships assists in identification and assessment of new drug and vaccine targets. Frequently, the molecular arsenal deployed by invading pathogens, and in particular parasites, reveals a common theme whereby families of proteins with conserved three-dimensional folds play crucial roles in infectious processes, but individual members of such families show high levels of specialisation, which is often achieved through grafting particular structural features onto the shared overall fold. Accordingly, the applicability of predictive methodologies based on the primary structure of proteins or genome annotations is limited, particularly when thorough knowledge of molecular-level mechanisms is required. Such instances exemplify the need for experimental three-dimensional structures provided by protein crystallography, which remain an essential component of this area of research. In the present article, we review two examples of key protein families recently investigated in our laboratories, which could represent intervention targets in the metabolome or secretome of parasites.


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