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GENTAUR Europe

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    Friday, 10 January 2014 10:24

    International Year of Crystallography

    INTERNATIONAL YEAR OF CRYSTALLOGRAPHY - 100 years since Nobel Prize for X–ray diffraction

    In 1914, the Nobel Prize in Physics was awarded to Max von Laue for making the connection between X–ray diffraction angles and the size and orientation of spacing between units in a crystal. In 2014, the United Nations General Assembly adopted a resolution proclaiming this year as the International Year of Crystallography. UNESCO and the International Union of Crystallography have been invited to facilitate this proclamation and have put together a year–long program.

    CRYO SHUTTER - Annealing is a promising technique to improve poorly diffracting crystals

    Cooling your sample to cryo–conditions helps protect the structure of a crystal from radiation and thermal motion. Poor cryo–cooling can increase the sample's mosaicity, leading to poor diffraction data. A brief interruption of the cryo–stream can warm then re–cool the crystal and potentially reduce mosaicity.
    The Cryo Shutter, developed by Dr. Uwe Mueller, MX-Lab at BESSY-II, HZB Berlin-Adlershoto is an automated system for crystal annealing, ready for installation on Cryojet (Oxford Instruments) and Cryostream 700 Systems (Oxford Cryosystems).

    Features:
    • Precise interruption of the cryostream
    • Reproducible crystal annealing
    • Extremely fast closing and opening of the shutter prevents turbulences

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    Order: IN SITU PLATE

    IN SITU PLATE - The revolutionary 96-well SBS format crystallization plate like no other

    The plate's design allows you to:
    • Use your current robot to populate
    • Setup sitting or hanging drops with the robot
    • You can choose from 1 to 6 growth drops per well
    • Use from 50 nl - 2 µl size drops
    • Obtain more hits and reproducible results
    • Use X-rays to screen crystals for diffraction before harvesting
    • Get better results from UV screening
    • Transport your crystals safely to the synchrotron

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    Order: IN SITU PLATE

    THE MICRORT™ SYSTEM - Easily screen crystals at room–temperature before cryoprotecting and freezing

    Room–temperature screening is especially important in protein crystallography, as many low–temperature data sets do not yield diffraction data of sufficient quality to determine a structure. MiTeGen’s patented MicroRT™ system allows you to screen your samples for improper crystal alignment due to damage or poor as–grown crystal quality before you head to the beamline. Introducing routine room-temperature screening of your crystals can easily save your experiment time, money, and effort.

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    Included:
    • 1 MicroRT™ Tubing Kit (20 1.5” (37 mm) long clear polyester capillaries sealed at one end; Extra–keen razor blades for cutting tubes to desired length; Small tube of grease for lubricating the base)
    • 1 MicroRT™ Aligner for properly setting the capillary tube over the crystal and onto the base
    • 1 box of 20 Dual-Thickness MicroMounts™
    • 1 pair of serrated-end tweezers

    Features:
    • Allows rapid screening of crystals at room temperature, to help maximize the efficiency of your crystallography pipeline.
    • Easy sample mounting with little risk of crystal loss or damage.
    • Easy collection of both room and low-temperature data from the same sample.
    • Easy sample visualization and alignment, especially for small crystals.
    • Capillary tubing is easily cut and sealed, and gives significantly less background X-ray scatter than glass capillaries.
    • One size capillary fits all, and capillaries are reusable, lowering your cost per measurement.

    Order: THE MICRORT SYSTEM

    Read more about Crystallography innovation

    More: IN SITU PLATEs

    Published in Promos

    Scientists have obtained the first detailed molecular structure of a member of the Tet family of enzymes.
    The finding is important for the field of epigenetics because Tet enzymes chemically modify DNA, changing signposts that tell the cell's machinery "this gene is shut off" into other signs that say "ready for a change."
    Tet enzymes' roles have come to light only in the last five years; they are needed for stem cells to maintain their multipotent state, and are involved in early embryonic and brain development and in cancer.
    The results, which could help scientists understand how Tet enzymes are regulated and look for drugs that manipulate them, are scheduled for publication in Nature.
    Researchers led by Xiaodong Cheng, PhD, determined the structure of a Tet family member from Naegleria gruberi by X-ray crystallography. The structure shows how the enzyme interacts with its target DNA, bending the double helix and flipping out the base that is to be modified.

    Epigenetics enigma resolved First structure of enzyme that removes methylation

    This is the structure of the Tet enzyme with DNA. Note the purple ball at the active site, close to which one DNA base is flipped out of the double helix. Also note the degree to which the double helix is bent. Credit: Xiaodong Cheng, Emory University

     

    "This base flipping mechanism is also used by other enzymes that modify and repair DNA, but we can see from the structure that the Tet family enzymes interact with the DNA in a distinct way," Cheng says.
    Cheng is professor of biochemistry at Emory University School of Medicine and a Georgia Research Alliance Eminent Scholar. The first author of the paper is research associate Hideharu Hashimoto, PhD. A team led by Yu Zheng, PhD, a senior research scientist at New England Biolabs, contributed to the paper by analyzing the enzymatic activity of Tet using liquid chromatography–mass spectrometry.
    Using oxygen, Tet enzymes change 5-methylcytosine into 5-hydroxymethylcytosine and other oxidized forms of methylcytosine. 5-methylcytosine (5-mC) and 5-hydroxymethylcytosine (5-hmC) are both epigenetic modifications of DNA, which change how DNA is regulated without altering the letters of the genetic code itself.
    5-mC is generally found on genes that are turned off or on repetitive regions of the genome. 5-mC helps shut off genes that aren't supposed to be turned on (depending on the cell type) and changes in 5-mC's distribution underpin a healthy cell's transformation into a cancer cell.
    In contrast to 5-mC, 5-hmC appears to be enriched on active genes, especially in brain cells. Having a Tet enzyme form 5-hmC seems to be a way for cells to erase or at least modify the "off" signal provided by 5-mC, although the functions of 5-hmC are an active topic of investigation, Cheng says.
    Alterations of the Tet enzymes have been found in forms of leukemia, so having information on the enzymes' molecular structure could help scientists design drugs that interfere with them.
    N. gruberi is a single-celled organism found in soil or fresh water that can take the form of an amoeba or a flagellate; its close relative N. fowleri can cause deadly brain infections. Cheng says his team chose to study the enzyme from Naegleria because it was smaller and simpler and thus easier to crystallize than mammalian forms of the enzyme, yet still resembles mammalian forms in protein sequence.
    Mammalian Tet enzymes appear to have an additional regulatory domain that the Naegleria forms do not; understanding how that domain works will be a new puzzle opened up by having the Naegleria structure, Cheng says.

    Published in News