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Neutron Protein CrystallographyHydrogen, Protons, and Hydration in Bio-macromolecules$
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Nobuo Niimura and Alberto Podjarny

Print publication date: 2011

Print ISBN-13: 9780199578863

Published to Oxford Scholarship Online: May 2011

DOI: 10.1093/acprof:oso/9780199578863.001.0001

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Experimental procedure for neutron protein crystallography

Experimental procedure for neutron protein crystallography

Chapter:
(p.50) Part II Experimental procedure for neutron protein crystallography
Source:
Neutron Protein Crystallography
Author(s):

Nobuo Niimura

Alberto Podjarny

Publisher:
Oxford University Press
DOI:10.1093/acprof:oso/9780199578863.003.0002

This part focuses on the details of the experimental procedures of neutron protein crystallography (NPC). The technique of growing a large single crystal of protein is both indispensable for NPC and very difficult; therefore, a rigorous method of growing a crystal in the metastable region of the crystallization phase diagram is described. Also, special techniques for preparing samples, such as deuteration and cryogenic cooling, are given. Next are presented the three main types of NPC diffractometers currently used in the world—namely, the BIX, LADI, and TOF types—along with corresponding measurement details, such as calculations for the minimum amount of irradiation time needed and the total angular range through which the crystal must be rotated. The chapter finishes with concrete descriptions of the data-reduction procedure and the method to determine mobile hydrogen atoms, protonation/deprotonation states of ionized amino acid residues, and hydrogen atoms in water molecules.

Keywords:   crystallization phase diagram, large single crystal, quality of crystals, deuterated proteins, H/D exchange, protonation/deprotonation, X/N joint refinement

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