Open AccessNew methodologies at PF AR‐NW12A: the implementation of high‐pressure macromolecular crystallography
Author(s) -
Chavas Leonard Michel Gabriel,
Nagae Tadayuki,
Yamada Hiroyuki,
Watanabe Nobuhisa,
Yamada Yusuke,
Hiraki Masahiko,
Matsugaki Naohiro
Publication year - 2013
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s0909049513020797
Subject(s) - hydrostatic pressure , macromolecule , high pressure , protein crystallization , chemistry , synchrotron , chemical physics , nanotechnology , crystallography , materials science , crystallization , physics , engineering physics , biochemistry , thermodynamics , organic chemistry , nuclear physics
The macromolecular crystallography (MX) beamline AR‐NW12A is evolving from its original design of high‐throughput crystallography to a multi‐purpose end‐station. Among the various options to be implemented, great efforts were made in making available high‐pressure MX (HPMX) at the beamline. High‐pressure molecular biophysics is a developing field that attracts the interest of a constantly growing scientific community. A plethora of activities can benefit from high pressure, and investigations have been performed on its applicability to study multimeric complex assemblies, compressibility of proteins and their crystals, macromolecules originating from extremophiles, or even the trapping of higher‐energy conformers for molecules of biological interest. Recent studies using HPMX showed structural hydrostatic‐pressure‐induced changes in proteins. The conformational modifications could explain the enzymatic mechanism differences between proteins of the same family, living at different environmental pressures, as well as the initial steps in the pressure‐denaturation process that have been attributed to water penetration into the protein interior. To facilitate further HPMX, while allowing access to various individualized set‐ups and experiments, the AR‐NW12A sample environment has been revisited. Altogether, the newly added implementations will bring a fresh breath of life to AR‐NW12A and allow the MX community to experiment in a larger set of fields related to structural biology.