CRYSTALLOGRAPHIC ANALYSES OF LYSOZYME AND COLLAGENASE MICROGRAVITY GROWN CRYSTALS VERSUS GROUND CONTROLS

Citation
I. Broutin et al., CRYSTALLOGRAPHIC ANALYSES OF LYSOZYME AND COLLAGENASE MICROGRAVITY GROWN CRYSTALS VERSUS GROUND CONTROLS, Journal of crystal growth, 181(1-2), 1997, pp. 97-108
Citations number
36
Categorie Soggetti
Crystallography
Journal title
ISSN journal
00220248
Volume
181
Issue
1-2
Year of publication
1997
Pages
97 - 108
Database
ISI
SICI code
0022-0248(1997)181:1-2<97:CAOLAC>2.0.ZU;2-1
Abstract
Hen egg white lysozyme and collagenase from Hypoderma lineatum larvae have been used as model proteins of known physical arid chemical prope rties to study the influence of microgravity on crystal quality. This was performed using the Advanced Protein Crystallization Facility inst rument during two successive missions of the US Space Shuttle. Lysozym e crystals were grown during the SpaceHab-01 mission and are compared with those obtained during the six months Eureca mission using the Pro tein Crystallization Facility instrument. Collagenase crystals were pr oduced during the IML-2 mission. Space grown crystals as well as groun ds controls were analyzed using synchrotron radiation to assess their diffraction limits. For lysozyme crystals, a large number of ground an d microgravity grown crystals were analyzed and showed nearly equivale nt maximum resolution (best one is 1.3 Angstrom). Collagenase crystals from IML-2, although presenting a marginal increase of resolution (1. 7 Angstrom), display a better signal to noise ratio than ground crysta ls.