br Experimental design materials and methods The preparation

Experimental design, materials, and methods The preparation of recombinant protein and crystallization for the periaxin PDZ (post-synaptic density-95, discs large, zona occludens-1)-like domain and the gliomedin olfactomedin (OLF) domain have been described [4,5]. Crystals of the periaxin PDZ-like domain were obtained in 30% polyethylene glycol (PEG) 2000 monomethyl ether, 0.1M KBr at +4°C, and tungsten derivatization was completed by soaking the crystals in 5mM (NH4)2WS4 for 2 days, while Xe-derivatized crystals were prepared at the beamline, by incubating fresh crystals in a Xe chamber at 200psi for either 2 or 8min. A gliomedin OLF domain crystal, grown in 0.1M CHES (pH 9.5) containing 20% PEG 8000, was derivatized with platinum by soaking in 5mM K2PtCl4 at room temperature. All diffraction data were collected on the synchrotron BMS-754807 beamline 14.1 at BESSY (Berlin) and processed with XDS [3]. Data processing statistics are given in Table 1. The final crystal structures have been published elsewhere [1,2]. The periaxin structure can be solved using a MIRAS (multiple isomorphous replacement and anomalous scattering) approach with the peak wavelength data for tungsten and the 8-min xenon dataset, in phenix.autosol [6]. In addition, data for the tungsten derivative were collected at the inflection point and at a high-energy remote wavelength, and for xenon, a dataset was also collected after 2-min derivatization. The gliomedin structure can be solved using SAD (single-wavelength anomalous dispersion) from the attached single dataset of a platinum derivative crystal, for example with programs in the Auto-Rickshaw pipeline [7]. Anomalous signals of all the reported datasets are compared in Fig. 1. For xenon derivatization, the signal is much higher with the longer incubation in the pressure chamber. The anomalous signal in different datasets of the tungsten derivative also indicates expected behavior, with the highest signal at the peak wavelength. It should be possible to solve the structure with these data and a MAD (multi-wavelength anomalous dispersion) approach, too.
Acknowledgments Sincere thanks are directed towards the macromolecular crystallography beamline staff at BESSY. This work was financially supported by Academy of Finland(grant 252066),Sigrid Jusélius Foundation (Finland), andEmil Aaltonen Foundation (Finland).
Data description The raw data consists in initial rates from enzymatic reaction considering the substrate uncompetitive inhibition equation. This data was generated through simulation of the initial rate calculated from the substrate uncompetitive inhibition equation adding a relative error from a normal distribution with standard deviation 0.5. The analyzed data was a list of kinetic parameters , and obtained using the direct linear plot method [1,2]. The resulting data was the statistic estimators of , and calculated from the median of the previous list.
Experimental design and methods
Acknowledgements The authors Pedro Valencia and Carolina Astudillo-Castro want to thank the financial support from FONDECYT/Regular Project1161293. Pedro Valencia wants to thank the financial support from USM Project216.12.2.
Data The data contains information on SRM assays for 94 pre-selected Synechocystis sp. PCC 6803 proteins analyzed from unfractionated samples. Represented are i) the SRM results in a complete, processed Skyline document deposited in Panorama Public repository, ii) the raw data and transition lists deposited in the Peptide Atlas SRM Experiment Library (PASSEL) as well as iii) indexed peptide retention times, iv) MSstats input file and v) statistical information on the changes in expression levels described with this article. The proteins subjected to SRM analysis, were extracted from wild type and sufR deletion mutant strains grown under iron sufficient and deprived conditions.