Michael Becker

Brookhaven National Laboratory
From: 1996 - 2006

Past BNL Research Interests

My research interests are focused on developing and using X-ray crystallographic and other methods to investigate protein structure-function relationships in systems that are both intriguing from a scientific perspective, and of clear importance from a humanistic perspective. My current interests are:

I) Methods in membrane-protein structure determination

In a presentation to the Biology Working Group at the Workshop on Fourth Generation Light Sources held at Argonne National Laboratory on October 27-29, 1997, I proposed that it may be possible to determine structures of membrane proteins in 2-dimensional crystals by using hard X-ray from a Free Electron Laser, such as those planned for development at SSRL-SLAC and at DESY. I have since elaborated further on this proposal at several workshops and meetings, and I am pursuing feasibility and developmental studies, using current and evolving technologies, towards realizing this goal once useable X-ray FEL beams become available.

I am also interested in developing novel expression systems to obtain integral-membrane proteins in high yield for crystallographic and other studies.

II) Systems: Malaria, Photosynthesis/Solar Energy, Neurobiology

I have general and specific interests in the areas of malaria, photosynthesis/solar energy, and neurobiology, involving both membrane proteins and water-soluble proteins.

My main responsibility is to manage operations at the NSLS wiggler Beam Line X25, where I am the Spokesperson for Biomolecular Crystallography. Many members of our group contribute to supporting the beamline, including Lonny Berman, who is the Spokesperson for X25 overall, Shai Vaday and Steve Lamarra, who are the Local Contacts, and additional staff members. A list of publications from the beamline can be seen in the NSLS Publications Data Base for X25

Selected Past Publications

• Bai T., Becker M., Gupta A., Strike P., Murphy V.J., Anders R.F., and Batchelor A.H.
  Structure of AMA1 from Plasmodium falciparum reveals a clustering of polymorphisms that surround a conserved hydrophobic pocket.
  Proc Natl Acad Sci USA., 102(36):12736-12741 (2005).   PubMed   Full Text
  PDB file 1Z40   Jmol viewer
  See also BNL Press Realease of August 29, 2005.

• Becker M., Bunikis J., Lade B.D., Dunn J.J., Barbour A.G., and Lawson C.L.
  Structural investigation of B. burgdorferi OspB, a bactericidal Fab target.
  J Biol Chem., 280(17):17363-17370 (2005).   PubMed
  PDB files: 1RJL 1P4P   Jmol viewer
• Becker M., and Weckert E.
  On the possibility of determining structures of membrane proteins in two-dimensional crystals using X-ray Free Electron Lasers.
  In: Conformational Proteomics of Macromolecular Architecture. (R.H. Cheng, L. Hammar, editors), World Scientific Publishing, Singapore, pp. 133-147 (2004).
• Becker M., and Berman L.
  Frontiers in structural biology at high-brightness X-ray sources.
  Synchrotron Radiation News, 14:7-9 (2001).
• Becker M.
  Considerations on the possibility of using hard X-rays from a Free Electron Laser to determine structures of membrane proteins in 2-dimensional crystals.
  Potential Future Applications in Structural Biology of an X-ray Free Electron Laser at DESY
  pp. 184-198, EMBL, Hamburg (1999).
• Becker M.
  Preliminary considerations on the possibility of using hard X-rays from a Free Electron Laser to determine structures of membrane proteins in 2-dimensional crystals.
  Biophys J., 76:A121 (1999).
• Becker M., Stubbs M.T., and Huber R.
  Crystallization of phycoerythrin 545 of Rhodomonas lens using detergents and unusual additives.
  Protein Sci., 7:580-586 (1998).   PubMed   Full Text
• Becker M., Nagarajan V., and Parson W.W.
  Properties of the excited singlet states of bacteriochlorophyll a and bacteriopheophytin a in polar solvents.
  J Am Chem Soc., 113:6840-6848 (1991).
• Becker M., Nagarajan V., Middendorf D., Parson W.W., Martin J.E, and Blankenship R.E.
  Temperature dependence of the initial electron-transfer kinetics in photosynthetic reaction centers of Chloroflexus aurantiacus.
  Biochim Biophys Acta, 1057:299-312 (1991).

Last Modified: October 2, 2012
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