Macromolecular Crystallography

Overview 

The ability to determine the structure of proteins using X-ray crystallography has been one of the great scientific achievements over the past 50-60 years. It has provided broad insights into many areas of biology, ranging from the evolution of life to understanding the chemistry of enzyme catalysis to the control of cell growth and death. More recent applications have included producing the binding maps against which targeted drugs can be designed and evaluated, leading to unparalleled growth in effective, safe therapeutics. As such, X-ray crystallography is an essential tool for the PCCR to carry out its mission — to uncover the fundamental sources of cell growth anomalies associated with cancer and to develop new and effective therapeutics through structure-based drug design. 

Accordingly, the primary mission of the Macromolecular Crystallography Shared Resource (MM-SR) is to provide access to state-of-the-art technologies, hardware, and expertise to PCCR members who use X-ray crystallography to address cancer-related questions and develop anti-cancer therapeutics. Formally established as a shared resource in 1998, this resource has been committed to the support of macromolecular crystallography projects of PCCR researchers. The MM-SR has been a crucial resource to PCCR members studying cancer mechanisms and mutations, visualizing cancer-related drug targets and performing iterative, structure-based design of anti-cancer therapeutics. To enable the research of X-ray crystallography expert and nonexpert PCCR members, the MM-SR provides and maintains in-house equipment and computational resources for data collection and processing, robotic systems for high-throughput microcrystallization experiments and for their imaging and storage, and temperature-controlled rooms. 

The MM-SR’s services and support are critical to PCCR members’ research needs because X-ray crystallography requires that sophisticated and dedicated resources be immediately and locally available to researchers. Because of the high associated costs and the need for technical support, the X-ray data collection and crystallization hardware resources that the MM-SR provides are beyond the budgets and group size of most individual labs. 

This is especially true of the robotic crystallization and robotic visualization systems, which are key technologies that substantially accelerate the empirical process of identifying crystallization conditions and also allow, through microliter to nanoliter experiments, the preservation of precious biological material. By providing centralized hardware and expertise in a shared resource, the MM-SR makes these essential technologies widely available to PCCR members, promoting productivity and scientific interaction. 

Equipment 

For X-ray diffraction 

Two Rigaku RU-200 X-ray generators with Oxford cryosystems in an inverted phi arrangement:

  • First, with MSC Hires2 multilayer optics and an R-axis-IV++ image plate system optimized for use with a long unit cell axis that is characteristic of virus or membrane protein crystals.
  • Second, with MSC Blue optics and an R-axis-IV++ detector optimized for high flux to evaluate weakly diffracting protein crystals. 

Services and Pricing

PCCR Non-PCCR
X-ray Diffraction (per day) $ 45 $ 133
Siemens 1000A Machine $ 21 $ 21
Minstrel DT Imaging Robot,
Crystallization Rooms,
4DX Systems Crystal Spec,
Cryo-Xe-Siter,
Zeiss crystal microscopes,
Formulatrix visualization system with UV capability
Available at No Charge

Contact Information and Location

Calvin Steussy
Shared resource director
csteussy@purdue.edu
765-494-7249

TJ Schmidt
Shared resource director
765-496-3131

Location of Macromolecular Crystallography SR facility

Hockmeyer Hall of Structural Biology, Room 320