Biology Reference
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12
Interactive Crystallomic
Jan Sedzik*
Biologically important molecules have to be crystallized from solution before their
atomic structures can be determined. Once their structures have been determined,
reliable and fine structural details, which are crucial for structure-based drug design,
can be obtained. Crystallization is an important but very poorly understood process.
Our inability to produce good quality crystals is a severe limitation of protein crys-
tallography. In this chapter we present rational guidelines which aim to alter our
know-how on crystallization from “black magic” into quantitative and affordable
science. We have coined a new word, crystallomic , which can be applied to a
diverse range of molecules and may intensify research related to crystallogenesis.
Keywords: Crystallization; factorial design; crystallomic; proteins; virus; crys-
tals; crystallization screens.
Introduction
The most common procedure for uncovering structural information about
biological molecules is producing crystals. (The NMR technique plays a
minor role at this stage). Crystals are important for the production of struc-
ture-based drugs; however, accurate and reliable structures are only avail-
able when good quality crystals can be created. The acquisition of good
quality crystals is followed by computer-intensive analysis, leading to high-
resolution atomic details. Crystals are objects in which molecules are
*Protein Crystallization Facility, Department of Neurobiology, Care Sciences and Society,
NOVUM, Karolinska Institutet, Stockholm, Sweden, and Department of Chemical
Engineering and Technology, Protein Crystallization Facility, KTH, Teknikringen 28,
100 44 Stockholm, Sweden. E-mail: sedzik@swipnet.se.
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