An Unconventional Mode of Protein Crystal Growth: Case Study Xylanase

Mike Sleutel, Alexander Van Driessche, Dominique Maes

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


We report on the violation of the succession of crystal
growth modes as a function of supersaturation. Typically, a crystal
transitions from spiral growth to two-dimensional (2D) nucleation
mediated growth with increasing supersaturation. The defect-prone
monoclinic xylanase crystals studied in this work constitute an
exception to this well-maintained rule. This is the result of an unique
interplay between the dominating layer generation mechanism and the
subsequent occurrence and propagation of large numbers of lattice
discontinuities. The defect density becomes so high that, given enough
time, a fully developed, crystal-wide network of interlinked stacking
faults is generated. This network effectively abolishes any advancement
of steps emanating from the sole step source, being a spiral
dislocation. The crystals manage to recover from this growth cessation
by switching over to a secondary layer generating mechanism at lower supersaturation, that is, 2D nucleation. This work shows
that by simply departing from well-established purified protein model systems, one can obtain unconventional and highly
complex protein crystals with nontrivial growth mechanisms.
Original languageEnglish
Pages (from-to)2986-2993
JournalCrystal Growth & Design
Publication statusPublished - 2012


  • crystal growth
  • impurity
  • ostwald rule
  • stacking faults


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