Growth kinetics and motion of thaumatin crystals during USML-2 and LMS microgravity missions and comparison with earth controls

Lorber, Bernard; Ng, Joseph D.; Lautenschlager, P.; Giegé, Richard

doi:10.1016/s0022-0248(99)00398-x

Cited by 29 publications

(30 citation statements)

References 41 publications

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“…28,42 Nevertheless, this observation is insufficient to explain the results: the data in Figure 7B at approximately 20°C and 0.71-0.75 M tartrate spans a factor of almost ten in concentration.…”

Section: Sigma Thaumatinmentioning

confidence: 87%

“…For example, Kadri et al 30 report that when the pH is changed from 7.0 to 6.5, the solubility increases by 7%, while the results in Figure 7B change by more than a factor of 2 (the bowties are the results at pH 7.0; the cross is at pH 6.5). 42 (bowties and diamonds), Lorber et al 28 (cross), and Kadri et al 30 (circles). The conditions used for each set of data are summarized in Table 2.…”

Section: Sigma Thaumatinmentioning

confidence: 93%

“…28,30,33,42 Concentration measurements were carried out by UV-vis extinction spectroscopy on a Beckman-Coulter DU800 spectrophotomer. The extinction coefficient of thaumatin at 280 nm was taken to be E 0.1% ) 1.27 mg mL -1 cm -1 .…”

Section: Protein Purificationmentioning

confidence: 99%

“…The extinction coefficient of thaumatin at 280 nm was taken to be E 0.1% ) 1.27 mg mL -1 cm -1 . 28,44 Conductivity and pH measurements were performed using an Orion 4-Star conductivity and pH meter with a DuraProbe conductivity cell and a RossSure-Flow pH electrode (Thermo Fisher Scientific, Waltham, MA).…”

Section: Protein Purificationmentioning

confidence: 99%

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Effects of Protein Purity and Precipitant Stereochemistry on the Crystallization of Thaumatin

Asherie

Ginsberg

Greenbaum

et al. 2008

Crystal Growth & Design

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ABSTRACT:Thaumatin is frequently used as a model protein in crystallization studies because it rapidly forms crystals in the presence of tartrate ions. The thermodynamic and kinetic properties of thaumatin crystals have been studied for almost 10 years, and the results are contradictory. Here we show that by using a homogeneous preparation of thaumatin and controlling the stereochemistry of the tartrate precipitant, it is possible to achieve consistent results for the protein solubility. To understand the role of protein impurities in the crystallization of thaumatin, we examined two commercial sources of the protein and characterized the heterogeneities therein. To examine the effect of precipitant stereochemistry, we crystallized thaumatin with L, D, and DL (racemic) tartrate ions. We suggest that the inconsistencies among previous results stem in part from the different behavior of thaumatin with the L and D enantiomers: the solubility of thaumatin crystals increases with temperature in L-tartrate, whereas it decreases with temperature in D-tartrate. Our results demonstrate the importance of using pure protein and stereochemically pure precipitants in the crystallization of proteins.

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Section: Sigma Thaumatinmentioning

confidence: 87%

Section: Sigma Thaumatinmentioning

confidence: 93%

Section: Protein Purificationmentioning

confidence: 99%

Section: Protein Purificationmentioning

confidence: 99%

See 2 more Smart Citations

Effects of Protein Purity and Precipitant Stereochemistry on the Crystallization of Thaumatin

Asherie

Ginsberg

Greenbaum

et al. 2008

Crystal Growth & Design

View full text Add to dashboard Cite

show abstract

“…In a zero-gravity environment, such as on the International Space Station, three-dimensional suspensions of particles have been used in crystal growth [13,14]. It is found that stray vibrations (g-jitter) [15] generate undesirable hydrodynamic flows around the growing crystallites, which are known to reduce the quality of the resulting crystals [16].…”

mentioning

confidence: 99%