Protein Structure Determination: X-ray Crystallography Services by Creative Biostructure, Slides of Biology

X-ray crystallography is a widely used method for determining the three-dimensional structures of proteins and other macromolecules. Creative Biostructure offers X-ray crystallography services, from gene synthesis to structure determination, using state-of-the-art facilities and experienced scientists. The advantages of X-ray crystallography include high atomic resolution, applicability to various molecular weights, and the ability to reduce the technical barrier for difficult-to-process proteins. Creative Biostructure provides various crystallization strategies, including co-crystallization, bicelle-protein crystallization, lipidic cubic phase (LCP) crystallization, controlled in meso phase (CIMP) crystallization, trace fluorescent labeling crystallization, and crystallization chaperone strategies.

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2020/2021

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protein crystallography compa

nies

X-ray crystallography is currently the most favored

method for structural determination of proteins and other

macromolecules. The requisite for a successful X-ray

crystallographic application is to obtain single crystals of

the target protein. Data is then collected by diffracting X-

ray from the single crystal that has an ordered pattern of

atomic orientation. The assembly of atoms and molecules

in the crystal can be deduced from the measurement of

X-ray scattering.

At present, more than 120,000 protein structures

resolved by X-ray crystallography experiments have been

deposited in protein databank, accounting for nearly 90%

of the resolved proteins, suggesting the predominant

Featured Crystallization Services Feature Co-crystallization Co-crystallization retains the unique crystalline structures with their multiple components (e.g., proteins, DNA/RNA, chemical compounds, metal ions). Bicelle-Protein Crysta llization Providing a more bilayer-like environment for membrane proteins than in detergent micelles, enabling the use of standard crystallization screening methodology for membrane proteins. Lipidic Cubic Phase ( LCP) Crystallization LCP has a membrane-mimetic matrix suitable for stabilization and crystallization of membrane proteins in lipidic environment. Controlled In Meso Phase (CIMP) Crystal lization CIMP stabilizes membrane proteins in meso phase and allows for direct monitoring of phase transformation and crystallization events. Trace Fluorescent La beling Crystallization Great for the detection and identification of crystals by covalently labeling a fluorescent probe on the protein. Crystallization Chape rone Strategies Co-crystallization of challenging membrane protein targets with soluble protein chaperones. Crystallization with Mutant Library Appro aches Improvement of protein solubility and crystallization assisted by mutant library construction and screening.

Please feel free to contact us to discuss your project! References 1.D'Arcy A, et al. Microseed matrix screening for optimization in protein crystallization: what have we learned?. Acta Crystallographica Section F: Structural Biology Communications. 2014, 70(9): 1117-1126. 2.Hediger M R, et al. BioFET-SIM web interface: Implementation and two applications. PloS One. 2012, 7(10): e45379.

Related Sections Batch Screening for Crystal Production Bicelle-Protein Crystallization Co-crystallization Controlled In Meso Phase (CIMP) Crystallization Crystallization Chaperone Strategies Crystallization of Antibody-Antigen Complexes Crystallization with Mutant Library Approaches Lipidic Cubic Phase (LCP) Crystallization Membrane Protein Crystallization Optimization Screening Peptide Crystallization Trace Fluorescent Labeling Crystallization Viral Envelope Glycoprotein Crystallization Crystallography Data Analysis X-ray Diffraction Data Collection