Protein crystal growth—Microgravity aspects

doi:10.1016/S0273-1177(99)00725-5

Advances in Space Research

Volume 24, Issue 10, 1999, Pages 1231-1240

https://doi.org/10.1016/S0273-1177(99)00725-5 Get rights and content

Abstract

Protein crystals, grown under reduced gravity conditions, are either superior or inferior in their structural perfection than their Earth-grown counterparts. A reduction of the crystals' quality due to low-gravity effects on the growth processes cannot be understood from existing models. In this paper we put forth a rationale which predicts either advantages or disadvantages of microgravity growth. This rationale is based on the changes in the effective solute and impurity supply rates in microgravity and their effects on the intrinsic growth rate fluctuations that arise from the coupling of bulk transport to nonlinear interfacial kinetics and cause severe inhomogeneities. Depending on the specific diffusivity and kinetic coefficient of a protein and the impurities in the solution, either transport enhancement through forced flow or transport suppression under reduced gravity can result in a reduction of the kinetic fluctuations and, thus, growth with higher structural perfection. Investigating this mechanism of microgravity effects, we first demonstrate a one-to-one correspondence between these fluctuations, that are due to the bunching of growth steps, and the formation of defects in the crystals. We have confirmed the forced flow aspects of this rationale in ground-based experiments with lysozyme utilizing flowing solutions with varying, well characterized impurity contents.

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Citation Excerpt :
They can be minimized by maintaining steady external conditions, and adjusting the rate of transport to the growth interface, as suggested by our previous research.14,66,67 Transport rate acceleration can be achieved through forced flow of the solution,30 while transport is slower during, for instance, growth in microgravity.11,68 For a recent review on the mechanisms leading to such defects and for suggested modifications of the crystallization conditions that may help to avoid them, see Vekilov and Alexander.11
This chapter discusses the molecular mechanisms of defect formation. The goal of this chapter is to summarize the recent work on the molecular level on the processes that accompany crystallization, and lead to defects and associated lattice strain, and potential plastic deformations such as mosaicity. While the mechanisms leading to relatively perfect protein crystals have been studied in great detail at both the mesoscopic1-3 and the molecular level 4-8, only a few of the processes leading to defects have been monitored. This chapter demonstrates an argument that diffraction resolution is affected only by short-scale molecular disorder and not by mosaicity, striae, zoning, and block structures. On the other hand, the diffraction resolution is determined by the signal-to-noise ratio of high-index reflections. Finally, this chapter concludes by explaining that if the crystal consists of a few large blocks, the beam in X-ray diffraction experiments can be focused on only one of these blocks, and high-resolution structure determinationscan still be achieved.

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Protein crystal growth—Microgravity aspects

Abstract

J. Crystal Growth

J. Crystal Growth

Trends in Biotechnology

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

Structure

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

J. Crystal Growth

Oscillatory Zoning: A Pathological Case of Crystal Growth

Nature

The growth of large single crystals of lysozyme

Biopolymers

Atomic mechanisms in semiconductor liquid phase epitaxy