Neutron Laue macromolecular crystallography

Journal Article · Sun Jan 01 04:00:00 EST 2006 · European Biophysics Journal

DOI:https://doi.org/10.1007/s00249-006-0074-6· OSTI ID:930793

Meilleur, Flora ^[1]; Myles, Dean A A ^[2]; Blakeley, M. P. ^[3]

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1. Institut Laue-Langevin (ILL)
2. ORNL
3. European Molecular Biology Laboratory (EMBL), France

Recent progress in neutron protein crystallography such as the use of the Laue technique and improved neutron optics and detector technologies have dramatically improved the speed and precision with which neutron protein structures can now be determined. These studies are providing unique and complementary insights on hydrogen and hydration in protein crystal structures that are not available from X-ray structures alone. Parallel improvements in modern molecular biology now allow fully (per)deuterated protein samples to be produced for neutron scattering that essentially eradicate the large--and ultimately limiting--hydrogen incoherent scattering background that has hampered such studies in the past. High quality neutron data can now be collected to near atomic resolution ({approx}2.0 Angstroms) for proteins of up to {approx}50 kDa molecular weight using crystals of volume {approx}0.1 mm3 on the Laue diffractometer at ILL. The ability to flash-cool and collect high resolution neutron data from protein crystals at cryogenic temperature (15 K) has opened the way for kinetic crystallography on freeze trapped systems. Current instrument developments now promise to reduce crystal volume requirements by a further order of magnitude, making neutron protein crystallography a more accessible and routine technique.

• Research Organization: Oak Ridge National Laboratory (ORNL)
• Sponsoring Organization: SC USDOE - Office of Science (SC)
• DOE Contract Number: AC05-00OR22725
• OSTI ID: 930793
• Journal Information: European Biophysics Journal, Journal Name: European Biophysics Journal Vol. 35; ISSN EBJOE8; ISSN 0175-7571
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
CRYSTALLOGRAPHY
INCOHERENT SCATTERING
MOLECULAR BIOLOGY
MOLECULAR WEIGHT
NEUTRONS
PROTEIN STRUCTURE