منابع مشابه
Growth rates of protein crystals.
Protein crystallization is important for structural biology. The rate at which a protein crystallizes is often the bottleneck in determining the protein's structure. Here, we give a physical model for the growth rates of protein crystals. Most materials crystallize faster under stronger growth conditions; however, protein crystallization slows down under the strongest conditions. Proteins requi...
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Mineralogical processes taking place close to equilibrium, or with very slow kinetics, are difficult to quantify precisely. The determination of ultraslow dissolution/precipitation rates would reveal characteristic timing associated with these processes that are important at geological scale. We have designed an advanced high-resolution white-beam phase-shift interferometry microscope to measur...
متن کاملProtein crystal growth. Growth kinetics for tetragonal lysozyme crystals.
A method for immobilizing protein crystals has been devised for determining face growth rates, and used to investigate the growth kinetics of hen egg white lysozyme crystals. Growth rates were determined at 22 degrees C in 0.1 M sodium acetate, 5% NaCl, pH 4.0, on the visually identified (110) face of tetragonal lysozyme crystals. Protein concentrations ranged from 13 to 57 mg/ml (saturation co...
متن کاملGrowth inhibition of protein crystals: A study of lysozyme polymorphs
Crystal morphology is determined by the relative growth rates of the different faces involved. Opposite faces (hkl) and (h̄k̄l̄) can show different rates if the crystal structure does not have inversion symmetry. Protein crystals, being built of asymmetric molecules do not have identical opposite faces, except for those pairs linked by rotational symmetry. Here, we present an in-situ microscopy st...
متن کاملThe nacre protein perlucin nucleates growth of calcium carbonate crystals.
Atomic force microscopy (AFM) in aqueous solution was used to investigate native nacre of the marine snail Haliotis laevigata on the microscopic scale and the interaction of purified nacre proteins with calcium carbonate crystals on the nanoscopic scale. These investigations were controlled by scanning electron microscopy (SEM), light microscopy (LM) and biochemical methods. For investigations ...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2012
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja207336r