Alexei S. Soares
Brookhaven National Laboratory
Bldg. 463 - P.O. Box 5000
Upton, NY 11973-5000
Alexei Soares is 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.
Using highly accurate triplet phases measured with the three-beam method
to test and improve crystallographic data collection and refinement methods.
Developing methods to measure multiple triplet phases simultaneously,
while still maintaining sufficient accuracy for phasing structures after conventional
phasing methods have failed. An accurate "one at a time" triplet phase data
set was designed to be sensitive to the correctness of the insulin solvent,
and we invite collaborators to evaluate models against this hydration probe.
Investigating protein hydration and the role of water in protein function
by solving protein structures at high-resolution and on an absolute electron
density scale, as well as by applying high-pressure crystallographic methods
currently under development.
Click on above image to view the
3-Beam Diffractometer in action.
As part of the mail-in crystallography team of the PXRR - along with
Annie Héroux and
Howard Robinson -
I carry out extensive crystal screening and data collection efforts for the benefit of remotely
participating crystallographers. When collaborations can be established with these groups, concentrated
efforts are made to derive initial structure solutions.
To augment the mail-in program, and particularly the scouting for the best-in-the-lot crystal in these
projects, I promote the use of our cryogenic specimen automounters.
I work with visiting and mail-in crystallographers in carrying out robot-based data collections
using the combined capabilities of the bending magnet beam line
X12B and the undulator beam line
I develop and test methods for remote data collection based on the dna-suite of programs.
In addition, I assist outside investigators in efficient data collection and structure solving at
beam line X12B which I
manage jointly with D. Schneider. To further augment PXRR capabilities I embarked in building a program
and facilities for the high-pressure freezing of crystals. Encouraging diffraction measurements on
cubic and hexagonal insulin crystals frozen at high pressures at McChess and measured at BNL, indicate the
significant reduction in mosaic disorder that can be achieved by this strikingly simple, but tecnologically
Podzelinska K., He S., Soares A., Zechel D., Hove-Jensen B. and Jia Z.
Expression, purification and preliminary diffraction studies of PhnP.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F64(Pt 6):554-557 (2008).
Salameh M., Soares A., Hockla A. and Radisky E.
Structural basis for accelerated cleavage of bovine pancreatic trypsin inhibitor (BPTI) by human mesotrypsin.
J Biol Chem., 283(7):4115-23 (2008).
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).
Zhao X., Copeland D., Soares A. and West A.
Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of
SLN1 bound to a phosphoryl analog.
J. Mol. Biol., 375(4):1141-1151 (2008).
Carra J.H., McHugh C.A., Mulligan S., Machiesky L.M., Soares A.S. and Millard C.B.
Fragment-based identification of determinants of conformational and spectroscopic change at the ricin active site.
BMC Struct. Biol., 7:72 (2007).
Hewitson K.S., Lienard B.M., McDonough M.A., Clifton I.J., Butler D.,
Soares A.S., Oldham N.J., McNeill L.A. and Schofield C.J.
Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor
hydroxylases by tricarboxylic acid cycle intermediates.
J. Biol. Chem., 282(5):3293-3301 (2007).
Soares A.S., Carlucci-Dayton M., Robinson H., Sweet, R. and Schneider D.
Automation program for macromolecular crystallography at the NSLS.
American Crystallography Association Annual Meeting, Salt Lake City, (2007).
Copeland D.M., Soares A.S., West A.H. and Richter-Addo G.B.
Crystal structures of the nitrite and nitric oxide complexes of horse heart myoglobin.
J. Inorg. Biochem., 100(8):1413-1425 (2006).
Robinson H., Soares A.S., Becker M., Sweet R. and Heroux A.
Mail-in crystallography program at Brookhaven National Laboratory's National Synchrotron Light Source.
Acta Cryst., D62(11):1336-1339 (2006).
Skinner J.M., Cowan M., Buono R., Nolan W., Bosshard H., Robinson H.H., Heroux A., Soares A.S., Schneider D.K. and Sweet R.M.
Integrated software for macromolecular crystallography synchrotron beamlines II: revision, robots and a database
Acta Cryst., D62(11):1340-1347 (2006).
Soares A.S. and Y. Vekhter.
Experimental methods for measuring accurate high-amplitude phases and their importance in isomorphous replacement experiments.
Acta Cryst., D61(11):1521-1527 (2005).
Lovelace J., Soares A., Bellamy H., Sweet R., Snell E. and Borgstahl G.
First results of digital topography applied to macromolecular crystals.
J Appl Cryst., 37:481-485 (2004).
Makowski L. and Soares A.
Estimating the diversity of peptide populations from limited sequence data.
Bioinformatics, 19(4):483-489 (2003).
Soares A.S., Caspar D.L.D., Weckert E., Héroux A., Hölzer K., Schroer K., Zellner J., Schneider D., Nolan W. and Sweet R.M.
Three beam interference is a sensitive measure of the efficacy of
macromolecular refinement techniques.
Acta Cryst., D59(10):1716-1724 (2003).
Rodi D.J., Soares A.S. and Makowski L.
Quantitative assessment of peptide sequence diversity in M13 combinatorial peptide phage display libraries.
J Mol Biol., 322:1039-1052 (2002).
Last Modified: September 15, 2011
Please forward all questions about this site to: