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Instruments / Technical Area	Publication Details	Published
I24-Microfocus Macromolecular Crystallography	Exploiting fast detectors to enter a new dimension in room-temperature crystallography Robin L. Owen , Neil Paterson , Danny Axford , Jun Aishima , Clemens Schulze-Briese , Jingshan Ren , Elizabeth E. Fry , David I. Stuart , Gwyndaf Evans Acta Crystallographica Section D Biological Crystallography 70, 1248 - 1256 DOI: 10.1107/S1399004714005379 PMID: 24816094 Diamond Proposal Number(s): [5968] Open Access Show Abstract ▼ Abstract: A departure from a linear or an exponential intensity decay in the diffracting power of protein crystals as a function of absorbed dose is reported. The observation of a lag phase raises the possibility of collecting significantly more data from crystals held at room temperature before an intolerable intensity decay is reached. A simple model accounting for the form of the intensity decay is reintroduced and is applied for the first time to high frame-rate room-temperature data collection.	May 2014
	Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures Alke Meents , Sascha Gutmann , Clemens Schulze-Briese , Armin Wagner Proceedings Of The National Academy Of Sciences 107 (3), 1094-1099 DOI: 10.1073/pnas.0905481107 Open Access Show Abstract ▼ Abstract: Radiation damage is the major impediment for obtaining structural information from biological samples by using ionizing radiation such as x-rays or electrons. The knowledge of underlying processes especially at cryogenic temperatures is still fragmentary, and a consistent mechanism has not been found yet. By using a combination of single-crystal x-ray diffraction, small-angle scattering, and qualitative and quantitative radiolysis experiments, we show that hydrogen gas, formed inside the sample during irradiation, rather than intramolecular bond cleavage between non-hydrogen atoms, is mainly responsible for the loss of high-resolution information and contrast in diffraction experiments and microscopy. The experiments that are presented in this paper cover a temperature range between 5 and 160 K and reveal that the commonly used temperature in x-ray crystallography of 100 K is not optimal in terms of minimizing radiation damage and thereby increasing the structural information obtainable in a single experiment. At 50 K, specific radiation damage to disulfide bridges is reduced by a factor of 4 compared to 100 K, and samples can tolerate a factor of 2.6 and 3.9 higher dose, as judged by the increase of Rfree values of elastase and cubic insulin crystals, respectively.	Jan 2010
NONE-No attached Diamond beamline	Crystal structure of Ultralente - a microcrystalline insulin suspension Armin Wagner , Joachim Diez , Clemens Schulze-Briese , Gerd Schluckebier Proteins: Structure, Function, And Bioinformatics 74 (4), 1018-1027 DOI: 10.1002/prot.22213 Show Abstract ▼ Abstract: Ultralente insulin has been one of the commercially most important insulin preparations in diabetes treatment over the last 50 years. It is a suspension of insulin microcrystals which dissolve slowly following subcutaneous injection. Because of the small crystal size of about 25 × 25 × 5 ?m3 the atomic structure has been elusive until now. Here we present the crystal structures from Ultralente and their precursor microcrystals from the industrial manufacturing process. During this process insulin undergoes a conformational change within the microcrystals. Both structures show canonical folding of the insulin molecules but exhibit a number of new features when compared with other insulin structures. Surprisingly, we found that the Ultralente crystals bind the conservation agent methylparaben, which slows down dissolution of the crystals and thus contributes to the long duration of action.	Jun 2008
	Reduction of X-ray-induced radiation damage of macromolecular crystals by data collection at 15 K: a systematic study A. Meents , A. Wagner , R. Schneider , C. Pradervand , E. Pohl , Clemens Schulze-Briese Acta Crystallographica Section D Biological Crystallography 63 (3), 302-–309 DOI: 10.1107/S0907444906053261 PMID: 17327667 Show Abstract ▼ Abstract: The cryocooling of protein crystals to temperatures of around 100 K drastically reduces X-ray-induced radiation damage. The majority of macromolecular data collection is therefore performed at 100 K, yielding diffraction data of higher resolution and allowing structure determination from much smaller crystals. However, at third-generation synchrotron sources radiation damage at 100 K still limits the useful data obtainable from a crystal. For data collection at 15 K, realised by the use of an open-flow helium cryostat, a further reduction of radiation damage is expected. However, no systematic studies have been undertaken so far. In this present study, a total of 54 data sets have been collected from holoferritin and insulin crystals at 15 and 90 K in order to identify the effect of the lower data-collection temperature on the radiation damage. It is shown that data collection at 15 K has only a small positive effect for insulin crystals, whereas for holoferritin crystals radiation damage is reduced by 23% compared with data collection at 90 K.	Mar 2007

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