A.Mølgaard
and
S.Larsen
(2004).
Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase.
Acta Crystallogr D Biol Crystallogr,
60,
472-478.
PubMed id: 14993671
DOI: 10.1107/S0907444903029767
Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase.
A.Mølgaard,
S.Larsen.
ABSTRACT
The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus
has been crystallized in two crystal forms, an orthorhombic and a trigonal
crystal form. In the orthorhombic crystal form, the covalently bound
carbohydrate at one of the two N-glycosylation sites is involved in crystal
contacts. The orthorhombic crystal form was obtained at pH 5.0 and the trigonal
crystal form at pH 4.5. In one case, the two crystal forms were found in the
same drop at pH 4.7. The differences in crystal packing in the two crystal forms
can be explained by the pH-dependent variation in the protonation state of the
glutamic acid residues on the protein surface.
Selected figure(s)
Figure 3.
Figure 3 An overlay of the orthorhombic (yellow) and the
trigonal (purple) crystal form at the trigonal AA and BB crystal
contacts. The figure was prepared using the program MOLSCRIPT
(Kraulis, 1991[Kraulis, P. (1991). J. Appl. Cryst. 24,
946-950.]).
The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2004,
60,
472-478)
copyright 2004.