Recent results and new hardware developments for protein crystal growth in microgravity

DeLucas, L.J.; Long, Marcus J. C.; Moore, Karen; Rosenblum, William M.; Bray, Terry; Smith, Craig D.; Carson, M. A.; Narayana, S.V.L.; Harrington, Michael; Carter, D.; Clark, Amanda D.; Nanni, Raymond G.; Ding, Junling; Jacobo-Molina, Alfredo; Kamer, Greg; Hughes, S.H.; Arnold, Erin K.; Einspahr, Howard; Clancy, L.L.; Rao, G Srinivasa; Cook, Paul F.; Harris, Ben G.; Munson, S.H.; Finzel, B.C.; McPherson, Alexander; Weber, Patricia C; Lewandowski, Frank; Nagabhushan, T. L.; Trotta, Paul P.; Reichert, Paul; Navia, Manuel A.; Wilson, Keith; Thomson, John A.; Richards, R.N.; Bowersox, K.D.; Meade, Charles; Baker, Elise; Bishop, Sanford P.; Dunbar, B.J.; Trinh, E. H.; Prahl, Joseph M.; Sacco, Albert; Bugg, Charles E.

doi:10.1016/0022-0248(94)90740-4

Cited by 65 publications

(22 citation statements)

References 11 publications

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“…1 The experiments are small, have low mass, can be remotely operated, and potentially have a high scientific and commercial payback. To date, growth of macromolecular crystals in microgravity has had mixed results, with enhancement in some studies [2][3][4][5] and no positive or even detrimental effects in others. [6][7][8] CEWL, a frequent flyer in microgravity crystallization programs, reflects this variation with reports of decreased mosaicity, 4,9 increased diffraction resolution, 10 marginal improvement, 11 and no effects.…”

Section: Introductionmentioning

confidence: 99%

Investigating the Effect of Impurities on Macromolecule Crystal Growth in Microgravity

Snell

Judge

Crawford

et al. 2001

Crystal Growth & Design

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Chicken egg-white lysozyme (CEWL) crystals were grown in microgravity and on the ground in the presence of various amounts of a naturally occurring lysozyme dimer impurity. No significant favorable differences in impurity incorporation between microgravity and ground crystal samples were observed. At low impurity concentration the microgravity crystals preferentially incorporated the dimer. The presence of the dimer in the crystallization solutions in microgravity reduced crystal size, increased mosaicity, and reduced the signal-to-noise ratio of the X-ray data. Microgravity samples proved more sensitive to impurity. Accurate indexing of the reflections proved critical to the X-ray analysis. The largest crystals with the best X-ray diffraction properties were grown from pure solution in microgravity.

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Section: Introductionmentioning

confidence: 99%

Investigating the Effect of Impurities on Macromolecule Crystal Growth in Microgravity

Snell

Judge

Crawford

et al. 2001

Crystal Growth & Design

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“…Subsequent reports of flight experiments [97,98] and hardware development [99] made little mention of convection measurement as a tool for understanding protein crystal growth. This problem was later considered in a comprehensive review of macromolecular crystallization [163].…”

Section: Spaceflight Experiments On Protein Crystal Growthmentioning

confidence: 99%

Imaging techniques for mapping solution parameters, growth rate, and surface features during the growth of crystals from solution

Verma

Shlichta

2008

Progress in Crystal Growth and Characterization of Materials

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“…A number of reports show that crystallization of macromolecules in microgravity does indeed improve the quality of crystals obtained, considered in different ways (e.g. McPherson, 1993;DeLucas et al 1994 (and references cited therein); Koszelak et al 1995;Helliwell et al 1995;Snell et al 1995;Chayen et al 19966).…”

Section: Crystallization In Microgravitymentioning

confidence: 99%

“…DeLucas et al 1994;Snyder et al 1991;Bosch et al 1992). An increasingly popular apparatus for flights is the Advanced Protein Crystallization Facility (APCF), built by Dornier under contract from the European Space Agency, which is now in the process of being upgraded to a 'Protein Crystallization Diagnostic Facility (PCDF)'.…”

Section: Crystallization In Microgravitymentioning

confidence: 99%

Trends and Challenges in Experimental Macromolecular Crystallography

Chayen

Boggon

Cassetta

et al. 1996

Quart. Rev. Biophys.

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Macromolecular X-ray crystallography underpins the vigorous field of structural molecular biology having yielded many protein, nucleic acid and virus structures in fine detail. The understanding of the recognition by these macromolecules, as receptors, of their cognate ligands involves the detailed study of the structural chemistry of their molecular interactions. Also these structural details underpin the rational design of novel inhibitors in modern drug discovery in the pharmaceutical industry. Moreover, from such structures the functional details can be inferred, such as the biological chemistry of enzyme reactivity. There is then a vast number and range of types of biological macromolecules that potentially could be studied. The completion of the protein primary sequencing of the yeast genome, and the human genome sequencing project comprising some 105 proteins that is underway, raises expectations for equivalent three dimensional structural databases.

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Recent results and new hardware developments for protein crystal growth in microgravity

Cited by 65 publications

References 11 publications

Investigating the Effect of Impurities on Macromolecule Crystal Growth in Microgravity

Investigating the Effect of Impurities on Macromolecule Crystal Growth in Microgravity

Imaging techniques for mapping solution parameters, growth rate, and surface features during the growth of crystals from solution

Trends and Challenges in Experimental Macromolecular Crystallography

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