ResourceSpectroscopy
CrystalQuick X: Optimized Platform for In-Situ Analysis of Protein Crystals
30 Oct 2012Automation of the working steps involved in X-ray analysis of protein crystals significantly improves the success rate and reduces the time required for structure determination. In-situ analysis is often compromised by crystallization plates generating significant background scatter and impacting the quality of the data. In this application note from Greiner Bio-One the unique features of the CrystalQuick™ X, a 96 well microplate especially suited for in-situ and UV analysis of protein crystals, are described. Its open geometry allows data to be collected directly in the plate within an angular range of up to 80° and an ultra-thin-walled well bottom minimizes background scattering significantly.
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X-ray CrystallographyX-ray crystallography is an analytical technique used to determine the arrangement of atoms in a crystal. Monochromatic x-rays are produced from a synchrotron or x-ray generator. An x-ray crystallography system uses a detector to measure the x-ray diffraction from the crystal. The information is used to generate a 3D image of the crystal.MicroplatesMicroplates are multi-well plates used to increase the throughput of biological investigations. The number of wells microplates contain can range from 6 to 3243 wells, with the 96-well format being the most commonly used. Microplates can come tailored for a range of applications including cell culture, PCR, filtration, storage, non-binding surface, protein crystallization, as well as pre-coated, deep well and normal Standard microplates. Additionally, options for microplate colors include clear , black, white or black with clear bottom and white with clear bottom for absorbance microplate reader applications. Find the best microplates for your lab in our peer-reviewed product directory: compare products, check customer reviews and receive pricing direct from manufacturers.Protein CrystallographyProtein crystallization is the process of crystallizing purified proteins for 3D structure analysis by x-ray crystallography. The main methods of protein crystallization include sitting drop, hanging drop and microbatch. It is important to control parameters such as pH, temperature and concentration. Following crystallization, detectors and software are used for data collection and analysis.X-Ray Diffraction and SpectroscopyX-Ray diffraction & spectroscopy are used in material characterization to discern the structure and elemental composition of a sample. X-Ray diffractometers (XRD) are superior instruments in elucidating the dimensional atomic structure of crystalline materials, including powders, thin films and single crystals. For large unit cells or ordered macromolecules, consider small-angle X-ray scattering (SAXS). X-ray spectroscopic techniques include X-ray fluorescence (XRF) and X-ray photoelectron spectroscopy (XPS), both providing simple and accurate methods for determining the elemental composition of a material. Energy dispersive (EDXRF) and wavelength dispersive (WDXRF) XRF spectrometers are available, as well as handheld/portable devices. High-resolution, 3D microstructure characterization of materials can be achieved with X-ray microscopes combining sub-micron resolution imaging with 3D computed tomography. Find the best XRD and XRF spectrometers in our peer-reviewed product directory: compare products, check customer reviews and receive pricing direct from manufacturers.Structural BiologyCrystallization