Argonne National Laboratory

The Advanced Protein Characterization Facility

The APCF is a new facility recently established at the Argonne National Laboratory. In a new building, the APCF provides laboratories for experimental characterization of proteins and larger macromolecular systems. Research activities are directed toward understanding the structure and function of proteins found in diverse biological systems, including soil and human microbiomes. The APCF utilizes high-throughput automated methods for bioinformatics, proteomics, molecular and structural biology. The APCF has expanded the capability to clone genes, express, produce and crystallize and fully characterize proteins and other macromolecules. Crystals are grown at nanoliter scale from hundreds of conditions and are delivered to beamlines at the Advanced Photon Source (APS) where data are collected and three-dimensional structures are often determined in near real time. The physical co-location of APCF with the APS is a unique feature at the US light sources. It allows expediting the transfer of pure proteins and crystals from the biochemistry and crystallography laboratories to the beamlines for rapid structural characterization.

The APCF also provides the environment needed to investigate protein function. Biochemical functions of proteins can be deciphered through a combination of bioinformatics, structural and experimental approaches. The capability to perform high-throughput protein function screening is critical to the advancement of biomedical, biotechnological and bioenvironmental research as discovery of protein functions is essential for diagnostics, therapeutics, and environmental studies.

The APCF, with the infrastructure and expertise, should accelerate characterization of proteins involved in major microbial pathways relevant to bio-energy and specialty chemical production, related to human pathogens, infectious diseases and antibiotic resistance, cancer, biotechnology, or homeland security bio threats. The APCF will advance the State of Illinois research and education in biological and biochemical sciences through the user facility component which will provide training in advanced protein chemistry methods in collaboration with local and state education organizations and will encourage participation through visiting scientist appointments.

Argonne collaborators:

  • Frank Collart – Molecular sensors
  • Phani Pokkuluri – Improving stability of Rubisco activase
  • Marianne Schiffer – Two-component systems
  • Christopher Henry – Microbial metabolism, enzyme promiscuity
  • Karolina Michalska – Marine sediments archaeal proteases
  • Youngchang Kim – Hypotheticals from select pathogens
  • Gyorgy Babnigg – Microfluidic devices in functional and structural biology

Outside collaborators:

  • George Phillips (Rice University) – Enzyme Discovery for Natural Product Biosynthesis
  • James Sacchettini (Texas A&M University) – Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors
  • Celia Goulding (University of California, Irvine) – Structure-Function Analysis of Polymorphic CDI Toxin-Immunity Protein Complexes
  • Joshua Adkins (Battelle Pacific Northwest Laboratories) – Characterization of Secreted Effector Proteins
  • Robert Haselkorn (University of Chicago) – Transcription regulation of heterocyst differentiation
  • Howard Shuman (University of Chicago, HTRL) – Legionella secreted effectors
  • Olaf Schneewind (University of Chicago, HTRL) – Virulence factors, Yersinia pestis hypotheticals
  • Steve Kent (University of Chicago) – Racemic crystallography
  • Sean Crosson (University of Chicago) – Brucella hypotheticals
  • Michelle O’Malley (Univ. of California, Santa Barbara) – Cellulases from anaerobic gut fungi
  • Matthias Hess (University of California, Davis) – Unusual cellulases
  • Kirsten Hofmockel (Iowa State University) – Carbon cycling core enzymes in soil aggregates
  • Tilman Schirmer (University of Basel) – EAL proteins
  • Steve Winans (Cornell University) – Plant transcription factors
  • Amy Gladfelter (Dartmouth College) – RNA-binding proteins
  • John Mekalanos (Harvard Medical School) – Type VI effectors
  • Wei Zhang (Illinois Institute of Technology) – Listeria transcription factors
  • Kira Makarova (NCBI) – CRISPR proteins
  • James Shorter (University of Pennsylvania) – Hsp104 chaperone
  • Alexander Yakunin (University of Toronto) – Cas4 proteins
  • Alexander Ensminger (University of Toronto) – Legionella effectors
  • Alexei Savchenko (University of Toronto) – Legionella effectors
  • raig Roy (Yale School of Medicine) – Legionella effectors
  • Gary Stacey (University of Missouri) – Transcription factors
  • Lukasz Berlicki (Wroclaw University of Technology) – Glutamine synthetases
  • Tom Terwilliger (Los Alamos National Lab) – Essential enzymes
  • John Brumell (Hospital for Sick Children, Toronto, Canada) – Effector proteins
  • Michael E. Konkel (Washington State University) – Effector proteins
  • Francisco Barona-Gomez (LANGEBIO) – Enzyme promiscuity
  • Christine Orengo (University College London) – Human microbiome
  • Lizbeth Hedstrom (Brandeis University) – IMPDHs and their inhibitors
  • Gregory D. Cuny (University of Houston) – IMPDHs and their inhibitors
  • Yunje Cho (POSTECH, Korea) – DNA repair enzymes
  • Fraydoon Rastinejad (Sanford Burnham, FL) – Nuclear receptors
  • Theresa Koehler (The University of Texas Health Science Center at Houston) B. anthracis virulence regulator
  • Hung Ton-That (The University of Texas Health Science Center at Houston) C. diphteria sortases
  • Barbara Lipinska (The University of Gdansk) Human HtrA3 protease