Reference : A crystal of a typical EF-hand protein grown under microgravity diffracts X-rays beyo...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/59024
A crystal of a typical EF-hand protein grown under microgravity diffracts X-rays beyond 0.9 Å resolution
English
Declercq, Jean-Paul mailto [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Physique Moléculaire et de Cristallographie - CPMC > >]
Evrard, Christine mailto [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Physique Moléculaire et de Cristallographie - CPMC > >]
Carter, Daniel [New Century Pharmaceuticals, Huntsville > > > >]
Wright, Brenda [New Century Pharmaceuticals, Huntsville > > > >]
Etienne, Gérard [UPRESA, Montpellier > > > >]
Parello, Joseph [The Burnham Institute, La Jolla > > > >]
1999
Journal of Crystal Growth
Elsevier Science
196
595-601
Yes (verified by ORBi)
International
0022-0248
Amsterdam
The Netherlands
[en] Protein crystallization ; Microgravity ; Atomic resolution ; Parvalbumin ; Calcium binding protein
[en] We report on our recent observation that crystals of a typical EF-hand protein (parvalbumin or Pa; Ca-loaded component from pike muscle with isoelectric point 4.10) grown under microgravity conditions diffract X-rays to a resolution better than 0.9 Å. The crystals were grown in the US space shuttle and characterized at 100 K, using an X-ray synchrotron beam. An effective atomic resolution has been achieved and substates in the conformation of the protein are observed. Large crystals up to 3 mm were also obtained.
http://hdl.handle.net/2268/59024
http://www.elsevier.com/wps/find/journaldescription.cws_home/505670/description#description

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