Premium
Anomalous diffraction at ultra‐high energy for protein crystallography
Author(s) -
Jakoncic Jean,
Di Michiel Marco,
Zhong Zhong,
Honkimaki Veijo,
Jouanneau Yves,
Stojanoff Vivian
Publication year - 2006
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/s0021889806036387
Subject(s) - phaser , anomalous scattering , diffraction , resolution (logic) , crystallography , wavelength , electron density , scattering , x ray crystallography , lanthanide , materials science , protein crystallization , crystal (programming language) , electron diffraction , molecular physics , chemistry , optics , electron , physics , optoelectronics , crystallization , computer science , nuclear physics , ion , organic chemistry , artificial intelligence , programming language
Single‐wavelength anomalous diffraction (SAD), multiwavelength anomalous diffraction (MAD) and single isomorphous replacement with anomalous scattering (SIRAS) phasing at ultra‐high X‐ray energy, 55 keV, are used successfully to determine a high‐quality and high‐resolution experimental electronic density map of hen egg‐white lysozyme, a model protein. Several combinations, between single‐ and three‐wavelength, with native data were exploited to demonstrate that standard phasing procedures with standard equipment and software can successfully be applied to three‐dimensional crystal structure determination of a macromolecule, even at these very short wavelengths. For the first time, a high‐quality three‐dimensional molecular structure is reported from SAD phasing with ultra‐high‐energy X‐rays. The quality of the crystallographic data and the experimental electron density maps meet current standards. The 2.7% anomalous signal from three Ho atoms, at the Ho K edge, was sufficient to obtain a remarkable electron density and build the first lanthanide structure for HEWL in its entirety.