Large-volume Protein Crystal Growth for Neutron Macromolecular Crystallography

Overview

Journal Acta Crystallogr F Struct Biol Commun

Specialty Chemistry

Date 2015 Apr 8

PMID 25849493

Citations 14

Authors

Joseph D Ng

James K Baird

Leighton Coates

Juan M Garcia-Ruiz

Teresa A Hodge

Sijay Huang

Affiliations

Soon will be listed here.

Abstract

Neutron macromolecular crystallography (NMC) is the prevailing method for the accurate determination of the positions of H atoms in macromolecules. As neutron sources are becoming more available to general users, finding means to optimize the growth of protein crystals to sizes suitable for NMC is extremely important. Historically, much has been learned about growing crystals for X-ray diffraction. However, owing to new-generation synchrotron X-ray facilities and sensitive detectors, protein crystal sizes as small as in the nano-range have become adequate for structure determination, lessening the necessity to grow large crystals. Here, some of the approaches, techniques and considerations for the growth of crystals to significant dimensions that are now relevant to NMC are revisited. These include experimental strategies utilizing solubility diagrams, ripening effects, classical crystallization techniques, microgravity and theoretical considerations.

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