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Curr Opin Struct Biol. 2006 Oct;16(5):630-7. Epub 2006 Sep 11.

Neutron protein crystallography: current status and a brighter future.

Author information

1
Center for Structural Molecular Biology, Oak Ridge National Laboratory, PO Box 2008, TN 37831, USA. mylesda@ornl.gov <mylesda@ornl.gov>

Abstract

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.

PMID:
16963258
DOI:
10.1016/j.sbi.2006.08.010
[Indexed for MEDLINE]

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