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Synchrotron‐based macromolecular crystallography module for an undergraduate biochemistry laboratory course
Author(s) -
Stiers Kyle M.,
Lee Christopher B.,
Nix Jay C.,
Tanner John J.,
Beamer Lesa J.
Publication year - 2016
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s1600576716016800
Subject(s) - beamline , synchrotron , protein crystallization , crystallography , crystallization , diffraction , class (philosophy) , structural biology , resolution (logic) , x ray crystallography , set (abstract data type) , computer science , chemistry , physics , optics , biochemistry , programming language , artificial intelligence , beam (structure) , organic chemistry
This paper describes the introduction of synchrotron‐based macromolecular crystallography (MX) into an undergraduate laboratory class. An introductory 2 week experimental module on MX, consisting of four laboratory sessions and two classroom lectures, was incorporated into a senior‐level biochemistry class focused on a survey of biochemical techniques, including the experimental characterization of proteins. Students purified recombinant protein samples, set up crystallization plates and flash‐cooled crystals for shipping to a synchrotron. Students then collected X‐ray diffraction data sets from their crystals via the remote interface of the Molecular Biology Consortium beamline (4.2.2) at the Advanced Light Source in Berkeley, CA, USA. Processed diffraction data sets were transferred back to the laboratory and used in conjunction with partial protein models provided to the students for refinement and model building. The laboratory component was supplemented by up to 2 h of lectures by faculty with expertise in MX. This module can be easily adapted for implementation into other similar undergraduate classes, assuming the availability of local crystallographic expertise and access to remote data collection at a synchrotron source.