Publications
1997
Ng J D, Lorber B, Giege R, Koszelak S, Day J, Greenwood A, McPherson A
Comparative analysis of thaumatin crystals grown on earth and in microgravity Journal Article
In: Acta Crystallogr D Biol Crystallogr, vol. 53, no. Pt 6, pp. 724-733, 1997, ISBN: 11540583, (0907-4449 Journal Article).
Abstract | Links | BibTeX | Tags: Comparative Study Crystallization Crystallography/instrumentation/methods Crystallography, Non-P.H.S. Sweetening Agents/*chemistry *Weightlessness, Non-U.S. Gov't Support, U.S. Gov't, Unité ARN, X-Ray Particle Size Plant Proteins/*chemistry Space Flight/*instrumentation Support
@article{,
title = {Comparative analysis of thaumatin crystals grown on earth and in microgravity},
author = {J D Ng and B Lorber and R Giege and S Koszelak and J Day and A Greenwood and A McPherson},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11540583},
isbn = {11540583},
year = {1997},
date = {1997-01-01},
journal = {Acta Crystallogr D Biol Crystallogr},
volume = {53},
number = {Pt 6},
pages = {724-733},
abstract = {The protein thaumatin was studied as a model macro-molecule for crystallization in microgravity-environment experiments conducted on two US Space Shuttle missions (USML-2 and LMS). In this investigation, we have evaluated and compared the quality of space- and earth-grown thaumatin crystals using X-ray diffraction analyses, and characterized them according to crystal size, diffraction resolution limit and mosaicity. Two different approaches for growing thaumatin crystals in the microgravity environment, dialysis and liquid-liquid diffusion, were employed as a joint experiment by our two investigative teams. Thaumatin crystals grown in a microgravity environment were generally larger in volume and the total number of crystals was less, relative to crystals grown on earth. They diffracted to significantly higher resolution and with improved diffraction properties, as judged by relative plots of I/sigma versus resolution. The mosaicity of space-grown crystals was significantly less than that of crystals grown on earth. Increased concentrations of protein in the crystallization chambers in microgravity led to larger crystals. The data presented here lend further support to the idea that protein crystals of improved quality can be obtained in a microgravity environment.},
note = {0907-4449
Journal Article},
keywords = {Comparative Study Crystallization Crystallography/instrumentation/methods Crystallography, Non-P.H.S. Sweetening Agents/*chemistry *Weightlessness, Non-U.S. Gov't Support, U.S. Gov't, Unité ARN, X-Ray Particle Size Plant Proteins/*chemistry Space Flight/*instrumentation Support},
pubstate = {published},
tppubtype = {article}
}
The protein thaumatin was studied as a model macro-molecule for crystallization in microgravity-environment experiments conducted on two US Space Shuttle missions (USML-2 and LMS). In this investigation, we have evaluated and compared the quality of space- and earth-grown thaumatin crystals using X-ray diffraction analyses, and characterized them according to crystal size, diffraction resolution limit and mosaicity. Two different approaches for growing thaumatin crystals in the microgravity environment, dialysis and liquid-liquid diffusion, were employed as a joint experiment by our two investigative teams. Thaumatin crystals grown in a microgravity environment were generally larger in volume and the total number of crystals was less, relative to crystals grown on earth. They diffracted to significantly higher resolution and with improved diffraction properties, as judged by relative plots of I/sigma versus resolution. The mosaicity of space-grown crystals was significantly less than that of crystals grown on earth. Increased concentrations of protein in the crystallization chambers in microgravity led to larger crystals. The data presented here lend further support to the idea that protein crystals of improved quality can be obtained in a microgravity environment.