Open AccessIn‐house low‐resolution X‐ray crystallography
Author(s) -
Evans Gwyndaf,
Roversi Pietro,
Bricogne Gérard
Publication year - 2000
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444900008982
Subject(s) - resolution (logic) , ribosome , macromolecule , diffraction , crystallography , protein crystallization , lysozyme , x ray crystallography , tetragonal crystal system , low resolution , crystal (programming language) , materials science , chemistry , optics , crystallization , high resolution , physics , crystal structure , computer science , geology , biochemistry , rna , remote sensing , programming language , organic chemistry , artificial intelligence , gene
It is demonstrated that standard in‐house protein crystal X‐ray diffraction apparatus can be used to measure very low resolution reflections with only a few modifications. The apparatus and modifications are described in detail and tested on two different macromolecular crystal samples: lysozyme and the 30S ribosomal subunit. Contrast‐variation measurements on tetragonal hen egg‐white lysozyme demonstrate the potential usefulness of the apparatus in providing accurate data for the determination of macromolecular envelopes. In contrast, the measurement of very low resolution diffraction from crystals of the 30S ribosome subunit illustrates how in‐house facilities can provide data from small weakly diffracting crystals of a very large macromolecule.