PubMed · 12690388
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
Rudolf Tromp. 2003. Surface diffusion: Atoms go underground.. https://doi.org/10.1038/nmat869
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Experiments have been carried out to study the behavior of L-threonine (needle-like) crystals during agitated drying. For an L-threonine/water system the morphology of the crystals was monitored using light microscopy and image analysis. Analysis of the transient behavior of the crystal size and shape distribution showed that attrition and agglomeration took place simultaneously during the process. The variation of the operating conditions (temperature, agitation and vacuum) revealed that attrition dominated the drying process when the drying rate was low and/or the shear rate was high. For high drying rates and low shear rates, agglomeration became dominant. This study suggests that crystal redissolution had no significant impact on crystal morphology. It was also found that due to their needle-like shape, large L-threonine crystals were very sensitive to attrition. When attrition controlled the drying process, most of the particle size reduction took place below a critical moisture content of 4%. When agglomeration controlled the drying process, most of the crystal size enlargement occurred below a moisture content of 6%.
The Escherichia coli ytfG gene product, with NAD(P)H:quinone oxidoreductase activity, was crystallized by the hanging-drop vapour-diffusion method at 296 K. A 1.78 A data set has been collected using synchrotron radiation at Pohang Light Source, South Korea. The crystal belongs to the primitive trigonal system, with unit-cell parameters a = b = 81.7, c = 76.8 A. Analysis of the packing density shows that the asymmetric unit probably contains one monomer, with a solvent content of 48.8%.
The ribosome recycling factor from Mycobacterium tuberculosis has been crystallized. The monoclinic crystals, with 52.5% solvent content, contain one protein molecule in the asymmetric unit.