Reference : Protein crystallisation under microgravity conditions: What did we learn on TIM crystall...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/62716
Protein crystallisation under microgravity conditions: What did we learn on TIM crystallisation from the Soyuz missions?
English
MAES, D. [ > > ]
DECANNIERE, K. [ > > ]
ZEGERS, I. [ > > ]
VANHEE [ > > ]
SLEUTEL, M. [ > > ]
WILLAERT, R. [ > > ]
Van de Weerdt, Cécile mailto [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire >]
Martial, Joseph mailto [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire >]
DECLERCQ, J.-P. [ > > ]
Evrard, Christine mailto [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire >]
OTALORA, F. [ > > ]
GARCIA-RUIZ, J.-M. [ > > ]
2007
Microgravity Science and Technology
XIX
5/6
90-94
Yes (verified by ORBi)
0938-0108
[en] Protein ; crystallisation ; microgravity
[en] The protein Triose Phosphate Isomerase from the hyperthermophilic organism Thermotoga maritima was crystallised on board of the International Space Station in the framework of the Soyuz missions. In this paper we report on the scientific results obtained during these flights. Firstly it qas shown that different crystal forms for the same protein in the same crystallisation conditions, what is presumably due to a change in the rate at which supersaturation is achieved. Secondly, the X-ray qualité of the crystals grown in the ISS is superior to their ground control crystals. Mimicking microgravity on ground, by adding a small amourt of gel to avoid convection, also results in an improvement of X-ray quality. Nevertheless our analysis shows that the crystals obtained in this gelled ground environment are of inferior quality as compared to their space homologues. Finally we observed movement of crystals grown in the International Space Station, not only because of g-jitters but also due to residual accelerations. This has an important effect on concentration gradients of precipiants and therefore on the solubility of the protein.
Giga-Development and Stem Cells
http://hdl.handle.net/2268/62716

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