Joanne McCarthy

MxCuBE: a synchrotron beamline control environment customized for macromolecular crystallography experiments

MxCuBE is a beamline control environment optimized for the needs of macromolecular crystallography. This paper describes the design of the software and the features that MxCuBE currently provides.

Automation of sample mounting for macromolecular crystallography

A standard sample holder and vial for cryocooled macromolecular crystals has been defined for use with robotic sample changers. This SPINE standard sample holder is a modified version, with added features and specifications, of sample holders in common use. In particular, the SPINE standard meets the precision required for automatic sample exchange and includes a cap that is identified by a two-dimensional datamatrix code as well as an optional vial. At the ESRF, the sample holder standard is in use with the EMBL/ESRF/BM14 robotic sample changer (SC3) which is installed on eight beamlines. The SC3 can hold up to 50 crystals stored in five baskets. A datamatrix reader in the SC3 ensures safe management of the sample flow and facilitates fully automatic screening and characterization of samples. Tools for handling and transporting 50 samples in a dry shipping dewar have been developed. In addition to the SC3, the SPINE sample holder is currently compatible with a number of other robotic sample changers.

High-throughput sample handling and data collection at synchrotrons: embedding the ESRF into the high-throughput gene-to-structure pipeline

An automatic data-collection system has been implemented and installed on seven insertion-device beamlines and a bending-magnet beamline at the ESRF (European Synchrotron Radiation Facility) as part of the SPINE (Structural Proteomics In Europe) development of an automated structure-determination pipeline. The system allows remote interaction with beamline-control systems and automatic sample mounting, alignment, characterization, data collection and processing. Reports of all actions taken are available for inspection via database modules and web services.

Online collection and analysis of X‐ray fluorescence spectra on the macromolecular crystallography beamlines of the ESRF

X-ray fluorescence (XRF) measurements on solutions or crystals of biological macromolecules provide additional information that can be used in structure determination and/or refinement protocols. Here details are presented of an experimental setup, employed on all the ESRF Macromolecular Crystallography Group beamlines, that allows the online collection and qualitative analysis of XRF spectra. This experimental setup uses a highly attenuated beam and short exposures, meaning it is minimally destructive but retains high sensitivity.

Structure of the manganese superoxide dismutase from Deinococcus radiodurans in two crystal forms

The structure of the manganese superoxide dismutase (Mn-SOD; DR1279) from Deinococcus radiodurans has been determined in two different crystal forms. Both crystal forms are monoclinic with space group P2(1). Form I has unit-cell parameters a = 44.28, b = 83.21, c = 59.52 angstroms, beta = 110.18 degrees and contains a homodimer in the asymmetric unit, with structure refinement (R = 16.8%, R(free) = 23.6%) carried out using data to d(min) = 2.2 angstroms. Form II has unit-cell parameters a = 43.57, b = 87.10, c = 116.42 angstroms, beta = 92.1 degrees and an asymmetric unit containing two Mn-SOD homodimers; structure refinement was effected to a resolution of 2.0 angstroms (R = 17.2%, R(free) = 22.3%). The resulting structures are compared with that of Mn-SOD from Escherichia coli, with which they are shown to be essentially isostructural.

The care and nurture of undulator data sets

Undulator radiation is the X-ray source of choice for modern macromolecular crystallography beamlines. Here, the basic properties of undulator sources are described and it is indicated why they make such good X-ray sources for macromolecular crystallography. Collection of excellent data from these beamlines is not always straightforward; therefore, a number of rules are postulated for undulator data collection and guidelines are offered which will help to ensure a satisfactory experiment.

Technical Report: Automatic Experiments at the European Synchrotron Radiation Facility MX Beam-lines

During the last twenty years macromolecular crystallography (MX) has become the predominant tool for the investigation of structure/function relationships in biology. This is due to many technological advances and, in particular, improved access to synchrotron radiation (SR) sources, data from which has lead to ∼80% of the macromolecular crystal structures currently being deposited in the Protein Data Bank (PDB) (Figure 1, http://www.rcsb.org). The demand for synchrotron beam-time is also being fuelled by the funding of a number of structural genomics programmes [1], which, following an initial investment in protein production technology, have now contributed ∼1000 new structures to the PDB.

4 f spin density in the reentrant ferromagnet SmMn 2 Ge 2

The spin contribution to the magnetic moment in

ESRF: A Quest for Excellence in Service to Users

{\mathrm{SmMn}}_{2}{\mathrm{Ge}}_{2}

4fspin density in the reentrant ferromagnetSmMn2Ge2

has been measured by magnetic Compton scattering in both the low- and high-temperature ferromagnetic phases. At low temperature, the Sm site is shown to possess a large