Protein crystallization; Microgravity; Atomic resolution; Parvalbumin; Calcium binding protein
Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Declercq, Jean-Paul; Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Physique Moléculaire et de Cristallographie - CPMC
Evrard, Christine ; 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
Language :
English
Title :
A crystal of a typical EF-hand protein grown under microgravity diffracts X-rays beyond 0.9 Å resolution
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