Anand M. Saxena
Brookhaven National Laboratory
Anand Saxena was a beam line scientist in the
Macromolecular Crystallography Research Resource (PXRR) which provides
facilities and support at the National Synchrotron Light Source for the benefit
of outside and in-house investigators. The PXRR is supported by the
NIH's National Center for Research Resources and the DOE Office of Biological
and Environmental Research in its mission to create optimal facilities and
environments for macromolecular structure determination by synchrotron X-ray
diffraction. With a staff of about 24, the PXRR innovates new access
modes such as FedEx crystallography, builds new facilities, currently on the
X25 undulator, advances automation, develops remote participation software,
collaborates with outside groups, teaches novice users, and supports visting
investigators with 7day, 20 hours staff coverage.
I am interested in the techniques and methods of structure determination of membrane
proteins. Specifically, I use biochemical and biophysical techniques to study the
refolding of membrane proteins that are expressed as inclusion bodies in bacterial
expression systems. I work on optimizing a system that may be used for refolding
membrane proteins by comparing the various emerging methods, including the use of
additives that prevent protein aggregation. The work is focused on understanding
the role of lipids in refolding and on the biochemical requirements for stability
of membrane proteins in solution. A second goal is the development of empirical
approaches for the crystallization of membrane proteins by examining the size of
the protein-detergent micelle, its dependence on detergents of various types, and
the role of small molecule additives.
Beam Line Scientist at X12C:
Improving the performance and throughput of synchrotron beam lines is a goal that I share
with my collegues in the PXRR. My primary responsibility is to manage the efficient operation
of the macromolecular X-ray crystallography user program at
and to manage its ongoing upgrades and upkeep.
Local Contact at X25:
Currently I am also the local contact at X25 and manage its crystallography user program
including the scheduling of general users, rapid access requests, and the allocation of discretionary
beam time. During the X25 upgrades in 2006 considerable flexibility in scheduling and staff committment
will be required to keep the X25 program productive. Beginning with the installation of a new undulator
in January 2006, followed by the installation of a cryogenically cooled monochromator in May, and finally
a new focusing mirror by the end of 2006, the beam line is beeing redeveloped by a large staff into a
higher intensity smaller beam facility that will serve our user community well.
Management of Rapid Access Program:
In addition, I manage the PXRR Rapid Access Program that allows outside experimenters
to come to the NSLS within a week or two of applying for beam time.
This program has become extremely popular among the user community because it provides them with beam
time soon after they have been able to crystallize a protein. The fraction of beam time
on PX beamlines that is assigned through the Rapid Access program has more than doubled
within a year. Currently about 4 out of 5 visiting groups are rapid access visitors whose
runs are fitted into a daily adjusted operating schedule. Time on insertion device lines
is in high demand, but increasingly concurrent access to bending magnet facilities is
requested for screening and characterization of best-in-the-lot crystals followed by
efficient data collection on insertion device lines.
GU= General User proposals
RA = Total Rapid Access requests
ID = RA insertion device line requests
BM = RA bending magnet line requests
MIX = RA request for ID and BM line
Anand Saxena managed the Membrane Neutron Diffraction User Program
at the High Flux Beam Reactor until its closing in 1999. This effort
was centered on the H3B Membrane Neutron Diffractometer.
Soares A.S., Schneider D.K., Skinner J.M., Cowan M., Buono R., Robinson H.H., Heroux A.,
Carlucci-Dayton M., Saxena A., and Sweet R.M.
Remote access to the PXRR macromolecular crystallography facilities at the NSLS.
Synchrotron Radiation News, 21(5):17-23 (September, 2008).
Balakrishna A.M., Tan Y.Y., Mok H.Y., Saxena A.M. and Swaminathan K.
Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS.
Acta Crystallographica, F62(Pt. 1):1024-1026 (2006).
Characteristics of thin-film multilayer monochromator systems from ray-tracing calculations.
Nucl Instrum Methods Phys Res A, (2000).
Neutron focusing devices based on segmented thin-film multilayers.
Nuclear Instruments and Methods in Physics Research, A 454(2-3):440-451 (2000).
Bradshaw J.P., Bushby R.J., Giles C.C.D., Saunders M.R. and Saxena A.
The headgroup orientation of dimyristoylphosphatidylinositol-4-phosphate in mixed lipid bilayers: a neutron diffraction study.
Biochim. Biophys. Acta, 1329:124-138 (1997).
The origin and minimization of the critical-angle reflection from a thin-film multilayer monochromator.
J Appl Cryst, 30:138-146 (1997).
Pertsemlidis A., Saxena A.M., Soper A.K., Head-Gordon T. and Glaeser R.M.
Direct evidence for modified solvent structure within the hydration shell of a hydrophobic amino acid.
Proc Natl Acad Sci USA, 93:10769-10774 (1996).
Duff K.C., Gilchrist P.J., Saxena A.M. and Bradshaw J.P.
Neutron diffraction reveals the site of amantadine blockade in the influenza A M2 ion channel.
Virology, 202:287-293 (1994).
Phycocyanin aggregation: A small angle neutron scattering and size-exclusion chromatographic study.
J Mol Biol., 200:579-591 (1988).
Last Modified: June 16, 2009
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