Characterization of protein and virus crystals by quasi-planar wave X-ray topography: a comparison between crystals grown in solution and in agarose gel
B. Lorber et al., Characterization of protein and virus crystals by quasi-planar wave X-ray topography: a comparison between crystals grown in solution and in agarose gel, J CRYST GR, 204(3), 1999, pp. 357-368
Quasi-planar wave reflection profile and X-ray topography studies have been
done to characterize the mosaicity of solution- and gel-grown crystals of
three proteins, turkey egg-white (TEW) lysozyme, thaumatin, and a bacterial
aspartyl-tRNA synthetase (AspRS) as well as of one virus, tomato bushy stu
nt virus (TBSV). These materials are representative of a large range of mol
ecular weight, overall particle shapes, crystals habits, packings, and solv
ent contents. Measurements of the full-width at half-maximum (FWHM) of refl
ections show that these different crystals have all a weak mosaicity. Topog
raphs display the same features as those of the well-studied hen egg-white
(HEW) lysozyme crystals: misorientation generated at the seed level for TEW
lysozyme or thaumatin crystals and/or strains at growth sector boundaries
for AspRS crystals. No growth defects are evidenced for TBSV crystals. For
the study of crystals diffracting at lower resolution (AspRS and virus), a
less absorbant sample holder, which facilitates crystal positioning in the
X-ray beam, has been developed. The results obtained for solution- and gel-
grown crystals do not show important differences. However, for TEW lysozyme
and thaumatin crystals, one notices a larger dispersion of results in the
solution case and an overall tendency for improved reproducibility of quali
ty for gel-grown crystals. (C) 1999 Elsevier Science B.V. All rights reserv
ed.