IYCr Open Factory: Inviting Young Crystallographers to Europe - Status & Outlook

The STOE DECTRIS Xenocs OpenFactory will take place from 10 to 19 September 2014. Participants receive seven days of intensive training by STOE, DECTRIS and Xenocs staff and guest scientists in cooperation with the IUCr. The training will focus on teaching participants the relevant theoretical skillset as well as giving practical training. In Grenoble, the delegates will spend significant time at the ESRF (European Synchrotron) and will be trained in Small Angle X-ray scattering at Xenocs' headquarters. In Darmstadt, the participants will be trained in Single Crystal and Powder XRD at STOE's headquarter. Delegates will have the opportunity to visit beamlines and interact with scientists at ESRF. Starting on 18 September, all OpenFactory participants will join the STOE annual user meeting. The user meeting is a platform for the exchange of ideas among its participants as well as speeches to highlight recent research results. It will be a unique opportunity for OpenFactory participants to interact with highly experienced XRD users and to build up relevant networks. This presentation and poster will highlight the activity, the focus of the program and present the selected participants for the OpenFactory event. The intention is to update on the status of the OpenFactory, but even more important, to encourage similar activities within and after the International Year of Crystallography. In this context, the presenter will discuss any insights from the applications received, i.e. geographies with particular high interest in the OpenFactory, which could be used to follow up on the OpenFactory with future events.

PDF calculations from STOE STADI P Ag Kα1 low- and high-temperature data

An impressive comparison of G(r) calculated with PDFgetX2(1) from data of Naphthalen taken at room temperature with a Stoe Stadi P powder diffractometer in Transmission mode equipped with a Ag-tube, a Ge(111)-monochromator for pure Ag-Kα1-radiation (0.5594 Å) as well as the Dectris MYTHEN 1K with1mm chip size and from synchrotron data, beamline X17A, NSLS Brookhaven with a wavelength of 0.1839 Å, yields amazingly similar peak widths for both experiment sites. To observe the temperature dependence of this resolution, the same laboratory setup with an additional Oxford Cryosystems Cobra or a Stoe furnace has been chosen to compare the signal width as a function of T. Low temperature data for these PDF calculation experiments has been taken from LaB6 as a crystalline standard and Naphthalene as well known organic phase. In addition high temperature G(r)-data from Ammonium Nitride will be demonstrated.

The crystal structure of human Aldehyde Oxidase in native and inhibited forms

Aldehyde oxidases (AOX; E.C. 1.2.3.1) are molybdo-flavoenzymes with broad substrate specificity, oxidizing aldehydes and N-heterocycles. AOX belongs to the xanthine oxidase (XO) family of Mo-containing enzymes. The true physiological function of AOX is still unknown, although it is recognized to play a role in the metabolism of compounds with medicinal and toxicological relevance [1]. AOX importance has increased in recent years since it is substituting Cyt-P450 as the central drug-metabolizing system in humans. We have solved the 3D structure of mouse AOX3 to 2.9 Å resolution [2] that was the first structure of an aldehyde oxidase, providing important evidences on substrate and inhibitor specificities between AOX and XO. The complement of AOX proteins in mammals varies from one in humans (hAOX1) to four in rodents (mAOX1, mAOX3, mAOX4 and mAOX3L1) as a result of evolutionary genetic events. Due to this unusual complement of AOX genes in different animal species, conclusions regarding protein metabolism in humans cannot be taken exclusively from the mouse model. Using the human aldehyde oxidase (hAOX1) purified after heterologous expression in Escherichia coli we were able to crystallize it and solve its 3D structure to 2.7 Å resolution (submitted). In addition to the native protein we also solved the structure of an inhibited form of the enzyme to 2.6Å resolution. Analysis of the protein active site and comparison with the structure of the mouse isoform (mAOX3) allowed us to identity, for the first time, the unique features that characterize hAOX1 as an important drug-metabolizing enzyme. In spite of the similarities of both enzymes, they show marked and relevant differences at the Mo active site, substrate tunnel as well as at the FAD site. The ensemble of these structures provides important insights into the role of aldehyde oxidases, contributing to elucidate the clinical metabolism implications of hAOX1 in humans which has particular relevance for novel drug design studies.