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Contaminant inclusion into protein crystals analyzed by electrospray mass spectrometry and X‐ray crystallography
Author(s) -
FontecillaCamps Juan Carlos,
Halgand Frédéric,
Forest Eric,
Hirschler Joachim
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560070119
Subject(s) - lysozyme , crystallography , chemistry , protein crystallization , mass spectrometry , x ray crystallography , recrystallization (geology) , rnase p , diffraction , crystal structure , crystal (programming language) , crystallization , chromatography , biology , organic chemistry , biochemistry , physics , paleontology , rna , programming language , optics , gene , computer science
Abstract The inclusion of protein contaminants into crystals of turkey egg white lysozyme (TEWL) was investigated by electrospray mass spectrometry of the dissolved crystals. The results show that significant amounts of the structurally related contaminant hen egg white lysozyme (HEWL) are included in the crystals of TEWL. The structurally unrelated contaminant RNAse A, on the other hand, is not included. The X‐ray diffraction data statistics of a hybrid TEWL/HEWL crystal and an uncontaminated TEWL crystal were of similar quality. This indicates that, even though the crystals contain much higher levels of the contaminant than one would have expected after a recrystallization experiment, they are still suitable for X‐ray diffraction experiments. However, attempts to detect the presence of the contaminant in the crystal by crystallographic structure refinement did not yield conclusive results.