@article{OtreloCardosodaSilvaCorreiaSchwuchowetal.2014,
  author    = {Otrelo-Cardoso, Ana Rita and da Silva Correia, Marcia Alexandra and Schwuchow, Viola and Svergun, Dmitri I. and Romao, Maria Joao and Leimk{\"u}hler, Silke and Santos-Silva, Teresa},
  title     = {Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis},
  series = {International journal of molecular sciences},
  volume    = {15},
  journal   = {International journal of molecular sciences},
  number    = {2},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1422-0067},
  doi       = {10.3390/ijms15022223},
  pages     = {2223 -- 2236},
  year      = {2014},
  abstract  = {The periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli is a molybdenum enzyme involved in detoxification of aldehydes in the cell. It is an example of an heterotrimeric enzyme of the xanthine oxidase family of enzymes which does not dimerize via its molybdenum cofactor binding domain. In order to structurally characterize PaoABC, X-ray crystallography and small angle X-ray scattering (SAXS) have been carried out. The protein crystallizes in the presence of 20\% (w/v) polyethylene glycol 3350 using the hanging-drop vapour diffusion method. Although crystals were initially twinned, several experiments were done to overcome twinning and lowering the crystallization temperature (293 K to 277 K) was the solution to the problem. The non-twinned crystals used to solve the structure diffract X-rays to beyond 1.80 angstrom and belong to the C2 space group, with cell parameters a = 109.42 angstrom, b = 78.08 angstrom, c = 151.77 angstrom, = 99.77 degrees, and one molecule in the asymmetric unit. A molecular replacement solution was found for each subunit separately, using several proteins as search models. SAXS data of PaoABC were also collected showing that, in solution, the protein is also an heterotrimer.},
  language  = {en}
}
@article{SchulzMehrabiMuellerWerkmeisteretal.2018,
  author    = {Schulz, Eike C. and Mehrabi, Pedram and M{\"u}ller-Werkmeister, Henrike and Tellkamp, Friedjof and Jha, Ajay and Stuart, William and Persch, Elke and De Gasparo, Raoul and Diederich, Fran{\c{c}}ois and Pai, Emil F. and Miller, R. J. Dwayne},
  title     = {The hit-and-return system enables efficient time-resolved serial synchrotron crystallography},
  series = {Nature methods : techniques for life scientists and chemists},
  volume    = {15},
  journal   = {Nature methods : techniques for life scientists and chemists},
  number    = {11},
  publisher = {Nature Publishing Group (London)},
  address   = {London},
  issn      = {1548-7091},
  doi       = {10.1038/s41592-018-0180-2},
  pages     = {901 -- 904},
  year      = {2018},
  abstract  = {We present a 'hit-and-return' (HARE) method for time-resolved serial synchrotron crystallography with time resolution from milliseconds to seconds or longer. Timing delays are set mechanically, using the regular pattern in fixed-target crystallography chips and a translation stage system. Optical pump-probe experiments to capture intermediate structures of fluoroacetate dehalogenase binding to its ligand demonstrated that data can be collected at short (30 ms), medium (752 ms) and long (2,052 ms) intervals.},
  language  = {en}
}