Neutron protein crystallography: Current status and a brighter future

Journal Article · Sun Jan 01 04:00:00 EST 2006 · Current Opinion in Structural Biology

DOI:https://doi.org/10.1016/j.sbi.2006.08.010· OSTI ID:1003631

Myles, Dean A A ^[1]

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1. ORNL

Hydrogen atoms are rarely seen in X-ray protein crystal structures, but are readily visualized by neutron crystallography, even at typical (1.5-2.5A) resolutions. Recent advances in neutron beamlines and deuterium labeling technologies have dramatically extended the scale and range of structures studied. High-quality neutron data can be collected to near atomic resolution ( approximately 1.5-2.5A) for proteins of 50-175kDa molecular weight, from perdeuterated samples, from crystals with volumes of 0.1mm(3) and at cryogenic temperatures (15K). These structures are providing unique and complementary insights into hydrogen-bonding interactions, protonation states, catalytic mechanisms and hydration states of biological structures that are not available from X-ray analysis alone. The new generation of spallation neutron sources promises further 10-50-fold gains in performance.

• Research Organization: Oak Ridge National Laboratory (ORNL)
• Sponsoring Organization: SC USDOE - Office of Science (SC)
• DOE Contract Number: AC05-00OR22725
• OSTI ID: 1003631
• Journal Information: Current Opinion in Structural Biology, Journal Name: Current Opinion in Structural Biology Journal Issue: 0 Vol. 16
• Country of Publication: United States
• Language: English

Related Subjects

08 HYDROGEN
36 MATERIALS SCIENCE
ATOMS
CRYOGENICS
CRYSTAL STRUCTURE
CRYSTALLOGRAPHY
DEUTERIUM
HYDRATION
HYDROGEN
MOLECULAR WEIGHT
NEUTRON SOURCES
NEUTRONS
PERFORMANCE
PROTEINS
RESOLUTION
SPALLATION