University of Chicago
5640 South Ellis
Chicago, IL 60637
Grant No. P41 RR007707
Investigator and Contact
Keith Moffat, Ph.D.
773-702-2116; Fax: 773-702-0439
BioCARS梐 component of the Consortium for Advanced Radiation Sources (CARS)梚s operating Sector 14 at the
Advanced Photon Source at Argonne National Laboratory as a national user facility for synchrotron radiation
research. The scientific interests of BioCARS are crystallographic studies of viruses, ribosomes, and other
complexes with very large unit cells; studies of microcrystals; time-resolved crystallography; and scattering
from less-ordered biological systems. In all cases, the goal is to understand basic biological processes in
structural terms, a goal fundamental to the pharmaceutical and biotechnology industries as well as to basic
Design and construction of novel optical elements to deliver the brilliant X-ray beam to the crystals;
design and construction of all components necessary to equip one sector at the Advanced Photon Source
consisting of one insertion device and one bending magnet beamline; novel forms of X-ray detectors; and
strategies for the effective acquisition of precise MAD data and time-resolved data.
Appropriate hardware and software for experiments in the areas outlined. BioCARS also is
equipped with a Biosafety Level 3 facility for operation of all stations and control areas in
BSL2 or BSL3 modes.
Illinois Institute of Technology
3101 South Dearborn Street
Chicago, IL 60616
Grant No. P41 RR008630
Investigator and Contact
Thomas Irving, Ph.D.
312-567-3489; Fax: 312-567-3494
630-252-0549; Fax: 630-252-0545
BioCAT has constructed and now operates facilities at Argonne National Laboratory抯 Advanced Photon
Source (APS) as a national research resource for the study of the structure of partially ordered
biological molecules, complexes of biomolecules, and cellular structures under conditions similar to
those present in living cells and tissues. The goal of BioCAT抯 research is to determine the detailed
structure and mechanism of action of biological systems at the molecular level. The techniques employed
are X-ray fiber diffraction; X-ray solution scattering; and X-ray absorption spectroscopy, with an emphasis
on time-resolved and space-resolved studies and development of novel techniques.
Typical applications: X-ray diffraction of biological fibers such as muscle and collagen;
membrane/protein systems; solution scattering of proteins and nucleic acids; time-resolved
protein folding. XAFS studies of metalloproteins and their complexes; site-selective XAFS by
high-resolution emission spectroscopy; X-ray Raman spectroscopy; in situ spectroscopy and X-ray
scattering in tissues as they relate to disease processes. Instrumentation development. Novel
detector designs. Improved data acquisition, data evaluation, and robust data analysis methods.
APS undulator A beamline, fixed exit height, cryogenically cooled silicon monochromators, energy
range 3.5� KeV Si(111), 8� KeV Si(400) using the first harmonic, up to 70 KeV with the second harmonic
of Si(400); one-meter-long harmonic rejection/vertical focusing mirror, crystal horizontal sagittal focusing.
Rapid crystal change with dual monochromators. Quick scanning capability: QXAFS scans in seconds. Measured flux
at 7 KeV is ~5 times 1013 photons/sec into a focal spot that is vertically adjustable between <20 祄 to ~1 mm
vertical, and horizontally adjustable from <200 祄 to ~4 mm with full beam flux. Independent horizontal and
vertical focus. Smaller beams (micron scale) are available at reduced flux. 0.3� small-angle X-ray scattering
(SAXS) camera. Ionization chambers, large acceptance multilayer analyzer/detector for fluorescence XAFS and
microprobe, CCD, image plate, and high-rate linear multi-element detector for SAXS. Software for time-resolved
data acquisition; shortest time slicing interval in standard setup for XAFS and MED ~1 m. Apparatus for optical
monitoring of sample integrity; polarized XAFS goniometer; stopped flow system; low vibration closed-cycle
helium refrigerator for sample cooling. Sample preparation and characterization laboratory adjacent to
beamline; electronics laboratory. Workstation with data analysis software for XAFS and SAS. Periodic
Brookhaven National Laboratory
Department of Biology
Upton, NY 11973
Grant No. P41 RR012408
Robert M. Sweet, Ph.D.
631-344-3401; Fax: 631-344-3407
For current contact information, please check the resource
The focus of this resource is to advance the state of macromolecular crystallography (PX) at the
National Synchrotron Light Source (NSLS), with dissemination of research methods, designs, and
computer codes to other synchrotron sources around the world. The resource teaches a world-class
course in rapid synchrotron data collection for PX and structure solving. A summary of the resource
programs can be found at
There are five major research projects under way in the resource
(www.x12c.nsls.bnl.gov/rr_summary/rr_summary.html): Development of the wiggler beamline X25 for
macromolecular crystallography; development of a shared computing system from inexpensive commodity
computers; remote monitoring and operation of beamline processes; use of multilayer monochromators for
macromolecular crystallography; and three-beam phasing for macromolecular crystallography
Five NSLS beamlines are tied together in a consortium dedicated to PX. Two constructed with Department
of Energy funding in the early 1980s, X12-B and X12-C, support a wide range of outside users, who gain
access through the peer-reviewed General User Program of the NSLS, collaborators of the NCRR resource,
and users from within the Biology Department抯 research program. At least half of the beam time at the
wiggler beamline X25 is devoted to PX. Similarly, in collaboration with the biophysics group at Los Alamos
National Laboratory, X8-C was built up, and Cold Spring Harbor Laboratory, SUNY Stony Brook, and Georgia
Research Alliance joined the Biology Department of the Brookhaven National Laboratory to bring X26C online;
25% of these two beamlines� time is available to general users. All beamlines are equipped with CCD-based area
detectors, and three have four-circle diffractometers bearing the detectors. MAD phasing is performed routinely,
and study of very high resolution diffraction or very large unit cells is available.
- Murakami, K., Masuda, S., and Darst, S., Structural basis of transcription initiation: T.
aquaticus RNA polymerase holoenzyme at 4 � resolution. Science 296:1280�84, 2002.
- Zhou, Y., Morais-Cabral, J., et al., Chemistry of ion coordination and hydration revealed by a
K+ channel-Fab complex at 2.0 � resolution. Nature 414:43�, 2001.
Wilson Synchrotron Lab
Ithaca, NY 14853-8001
Grant No. P41 RR001646
Sol M. Gruner, Ph.D.
607-255-3441; Fax: 607-255-8751
Quan Hao, Ph.D.
607-254-8983; Fax: 607-255-9001
This resource, also known as MacCHESS, operates three insertion-device beamlines (stations A-1, F-1,
and F-2) at the Cornell High Energy Synchrotron Source (CHESS) devoted to macromolecular crystallography.
In addition, the resource supports additional bending magnet stations for part-time macromolecular X-ray
experiments. The resource specializes in large unit-cell diffraction, ultra-high resolution diffraction,
MAD phasing, rapid-throughput crystallography (structure-based drug design and structural genomics),
microdiffraction, multiple-beam diffraction, and software development.
Unit cells as large as 1400 � have been resolved. Diffraction to 0.72 � has been collected.
Structures as large as 370 KDa have been solved by MAD phasing. As many as 70 selenium atoms have
been located from anomalous data. Datasets from ideal crystals can be collected in a few seconds.
Typical exposure times vary from 5 to 120 seconds. The resource is sufficiently efficient to accommodate
hundreds of researchers each year.
All stations utilize CCD area detectors. Image plates are also available. Sample cryo coolers
are available at the three wiggler stations. Station A-1 is for monochromatic measurements; a
49-pole wiggler replaces the 24-pole wiggler. Station F-1 is a monochromatic X-ray station designed to
accommodate large unit-cell samples. The station is equipped with a biohazard containment facility
rated at the Biosafety Level 3. Station F-2 is a tunable facility designed for MAD phasing from which
the X-ray energy can be tuned from 7.9 to 16 KeV. A cold room is present on site; microscopes are
available at all stations. 3-D graphics are available on some computers. Over a dozen Alpha computers support data processing.
A data collection GUI provides ease in collecting the diffraction data. All station
hardware motors are controlled with simple software. X-ray diffraction data are analyzed
using the DPS/Mosflm and DENZO software.
Stanford Synchrotron Radiation Laboratory
Department of Chemistry
Stanford, CA 94305
Grant No. P41 RR001209
Keith O. Hodgson, Ph.D.
650-926-3153; Fax: 650-926-4100
Stanford Synchrotron Radiation Laboratory (SSRL) provides synchrotron radiation for research in
several fields, including structural molecular biology, for which about 9 stations are dedicated
with access through a peer-reviewed proposal mechanism. The NCRR resource, which operates in synergy
with programs funded by the Department of Energy, Office of Biological and Environmental Research, and
the National Institute of General Medical Sciences, explicitly provides R&D and dedicated user support
teams for research in macromolecular crystallography, X-ray absorption spectroscopy (XAS), and small-angle
X-ray scattering (SAXS).
State-of-the-art macromolecular crystallography data collection/data reduction stations are available
for high-throughput, high-resolution, MAD-phasing and monochromatic crystallography studies. XAS capabilities
include high-resolution multi-element detectors and low-temperature cryostats for dilute protein solution
studies on stations covering the energy range 2� keV. For SAXS, instrumentation for both static and rapid
mixing time-resolved solution scattering studies is provided. A low-angle single-crystal diffraction
system is also available.
Macromolecular crystallography: End-stations BL9-2 and BL1-5 are fully tunable with excellent energy
resolution for performing MAD experiments. Wiggler end-station BL9-2 has an energy range of 5.920 keV
(0.622.1 �) and is equipped with a Quantum 315 detector system. Bending magnet BL1-5 has an energy range of
5.916 keV and is equipped with a Quantum 4 detector. Wiggler side-stations BL11-1 and BL9-1 are tunable
and have sufficient energy resolution for many MAD/SAD experiments. BL11-1 is a PRT beamline with 33% general
user access and is equipped with a Quantum 315 detector. BL9-1 has an energy range of 12.5� keV (0.73�99 �)
and is equipped with a Quantum 4 detector, and will soon be upgraded to a Quantum 315. The wiggler side-station
BL7-1 operates at a fixed energy of 11.5 keV (1.08 �) and is equipped with a MAR-345 detector. Experiments are
carried out using the BLU-ICE interface. All beamlines (except 7-1) have automated screening systems that support
three 96-pin cassettes. Collaborative tools are available for remote data collection and processing. Variable
cryostats, cryotools, Xe/Kr derivatizers, microscopes, incubators, dewars, cold rooms, and stereo visualization
equipment are also provided.
Small-angle X-ray scattering: A multipurpose SAXS camera is available for use on a semi-dedicated wiggler
end-station (~75% of total beam time currently). A stopped-flow rapid mixer and a continuous-flow jet mixer
are available for time-resolved SAXS studies of proteins in solution. A very-low-angle single crystal
diffraction system (10�0 �) is available for macromolecular crystallography. Detectors include linear
and quadrant wire detectors and CCD detectors. Dedicated computer facilities, data acquisition and analysis
software are provided.
X-ray absorption spectroscopy: Two dedicated wiggler and five shared wiggler or bending magnet stations
are available, equipped with high-throughput/high-energy resolution 30- and 13-element Ge array detectors or
ionization chamber detectors for fluorescence measurements of biological samples in the sub-millimolar to
millimolar concentration range. Four liquid He cryostats are available for data collection at temperatures as
low as 4 K. Interactive software on dedicated computers allows users to measure and analyze AS data and display
results online. Micro-imaging and single-crystal XAS instrumentation is under development.
Department of Chemistry and Chemical Biology
Ithaca, NY 14853-1301
Grant No. P41 RR015301
Steven E. Ealick, Ph.D.
607-255-7961; Fax: 607-255-1227
607-255-1112; Fax: 607-255-1227
The Undulator Resource for Structural Biology is a planned facility for macromolecular crystallography
at Sectors 8 and 24 of the Advanced Photon Source at Argonne National Laboratory. The resource is overseen
by the Northeastern Collaborative Access Team (NE-CAT), which includes scientists from Columbia University,
Cornell University, Harvard University, the Massachusetts Institute of Technology, Memorial Sloan Kettering
Cancer Center, Rockefeller University, and Yale University. Research emphasis is placed on signal transduction,
DNA transcription initiation and regulation, cell cycle regulation, virus structure and function,
membrane proteins, protein folding, and enzyme structure and function. Many of the research projects
focus on how biological molecules interact to form large macromolecular complexes. The macromolecules
studied by NE-CAT often involve large unit cells, small crystals, weakly diffracting crystals, and crystals
with weak anomalous scattering. Construction of the undulator resource requires development of a novel dual
undulator design utilizing components developed by the Advanced Photon Source. Other technological research
will focus on diamond monochromators, focusing optics, methods of phase determination, radiation damage, X-ray
detectors, and crystallographic software.
The Undulator Resource for Structural Biology will provide advanced synchrotron beamlines for macromolecular
crystallography. The resource also provides laboratory space for protein production and crystallization and
office space for data analysis. Upon completion, the undulator resource will provide three high-brilliance
undulator beamlines and one bending magnet beamline. Each beamline will be equipped with X-ray detectors,
cryocoolers, and other instrumentation for X-ray diffraction.
8-BM (end-station): Currently in commissioning phase. Features include a precollimator mirror,
vertical offset, sagittally focusing monochromator (5� KeV, 2 eV bandpass), ADSC Quantum 315 detector,
Huber 515 Kappa goniometer, Oxford Cryojet.
24-ID (end-station): Planned for late 2003. Features include a vertical offset diamond monochromator
(5� KeV, 2 eV bandpass), Kirkpatrick朆aez focusing, target flux (1013 ph/s in 100 times 100
mm2 at 12 KeV).
24-ID (side-station): Planned for late 2004. Features include a horizontal offset diamond
transmission monochromator (9� KeV, 2 eV bandpass), Kirkpatrick朆aez focusing, target flux (1012 ph/s
in 100 times 100 mm2 at 12 KeV).
24-ID (fixed-wavelength side-station): Planned for late 2005. Features include a single-bounce
diamond monochromator (fixed 12 KeV, 2 eV bandpass), Kirkpatrick朆aez focusing, target flux (1012
ph/s in 100 times 100 mm2 at 12 KeV).
Other facilities: 8,000 square feet of laboratory and office space in LOM436, including biochemical and computing facilities.