DTT in Protein Crystallization: Preventing Dimerization for Better Crystals
Protein crystallization is a vital technique for determining the three-dimensional structure of proteins, offering invaluable insights into their function and mechanisms. A significant hurdle in obtaining high-quality protein crystals is the tendency for proteins to aggregate or form dimers, particularly those with exposed or reactive cysteine residues. DL-Dithiothreitol (DTT), also known as Cleland's reagent, is a widely used biochemical additive that helps mitigate this problem by maintaining thiol groups in their reduced state.
Proteins that contain free sulfhydryl groups are prone to forming intermolecular disulfide bonds, leading to dimer formation or aggregation. This aggregation can interfere with the ordered packing required for crystal lattice formation. DTT acts as a potent reducing agent, effectively cleaving any nascent disulfide bonds and ensuring that cysteine thiols remain free. By preventing the formation of these cross-links, DTT promotes the solubility and stability of monomeric protein, which is crucial for successful crystallization. When researchers look to buy DTT for crystallization studies, ensuring its purity is key.
Typically, DTT is added to protein solutions at concentrations ranging from 1-5 mM during the crystallization process. Its role is to keep the protein in a state amenable to forming stable crystals, free from aggregation. As a dedicated DTT manufacturer, we produce DL-Dithiothreitol with high purity (≥98%), ensuring that it effectively performs its intended function without introducing unwanted side reactions or impurities that could hinder crystallization. Our commitment to quality makes us a preferred DTT supplier in China for researchers engaged in structural biology.
For scientists aiming to purchase Cleland's reagent for protein crystallization, understanding the optimal conditions and concentrations is important. While DTT is highly effective, it can also be sensitive to oxidation. Therefore, using freshly prepared solutions or storing DTT appropriately is recommended. If your research involves protein structure determination and you need to buy DTT, consider our reliable product range, backed by stringent quality control. We offer competitive DTT prices and are a dependable source for your laboratory needs.
In summary, DL-Dithiothreitol is an essential tool for protein crystallization, primarily by preventing disulfide-mediated aggregation and dimerization. Its effectiveness in maintaining protein integrity makes it indispensable for structural biologists. By choosing high-purity DTT from a reputable DTT manufacturer, you can significantly enhance your chances of obtaining high-quality protein crystals. We are your trusted partner for all your biochemical reagent requirements.
Perspectives & Insights
Core Pioneer 24
“By choosing high-purity DTT from a reputable DTT manufacturer, you can significantly enhance your chances of obtaining high-quality protein crystals.”
Silicon Explorer X
“Protein crystallization is a vital technique for determining the three-dimensional structure of proteins, offering invaluable insights into their function and mechanisms.”
Quantum Catalyst AI
“A significant hurdle in obtaining high-quality protein crystals is the tendency for proteins to aggregate or form dimers, particularly those with exposed or reactive cysteine residues.”