GCPCC Publications

    Please contact us when you have a publication resulting from work done at the GCPCC PX beamline.

    Miller MD, Phillips GN Jr., White MA, Fox RO, Craft BC III

    The development of the GCPCC Protein Crystallography Beamline at CAMD.

    Application of Accelerators in Research and Industry -- Sixteenth Int'l Conf., J.L. Duggan and I.L. Morgan eds., 734-737 (2001). {PDF}

    The PX Beamline Collaboration and Publication Policy

    The increased use of synchrotron beamlines by inexperienced users, and use of mail-in procedures, requires that users be able to enlist technical and scientific support for their projects.  The GCPCC beamline staff must be able to get appropriate credit for their work.  The object of this document is to help users and beamline staff reach easy agreement about the extent of the staff's involvement with the user's project, and the sort of credit that should be given.  One can imagine two extremes: use of the beamline alone should be acknowledged with a statement of the beamline's name and it's funding agencies.  A sample acknowledgment paragraph has been prepared and may be used for this purpose.  On the other hand, extensive involvement in a project by GCPCC staff, with substantial effort on and off the beamline, obviously should be accompanied by joint authorship.  There are many gray areas in between, and this document is intended to address those.

    The traditional approach has users coming to the synchrotron to perform the data collection themselves.  This often involves standard training and maintenance, and some minimal scientific contribution provided by the beamline staff.  Typically this deserves the standard acknowledgment mentioned above.

    Occasionally the beamline staff becomes substantially involved with the user's experiment.  For instance, there may be a need to modify apparatus or software to allow an experiment to be performed, or there may be need to put substantial effort into working out experimental protocols, or helping to reduce and interpret the data.  Both parties should consider very carefully whether this warrants co-authorship.  In cases where the experiment really might not have been successful without this help, the beamline scientist probably should be a co-author.

    With increasing frequency, users are mailing their prepared specimens to the beamline for screening, experimental design, data collection and reduction, and preliminary analysis.  These users should consider that their obligation for conferring co-authorship is substantially greater than traditional beamline users.  In this case, the users depend on the expertise of the beamline scientists, firstly to perform the data collection, secondly to detect failures in the process, and thirdly to extract the very best out of the user's precious specimens.  The skill level required of the beamline staff is high and the responsibility is great.  The beamline scientist will need to make all the decisions about the experimental plan.  Therefore, mail-in experiments should be considered an opportunity for the user to invite the experimenter to join as a co-author on that project.

    Publication List

    Qiu C, Tarrant MK, Choi SH, Sathyamurthy A, Bose R, Banjade S, Pal A, Bornmann WG, Lemmon MA, Cole PA, Leahy DJ
    Mechanism of activation and inhibition of the HER4/ErbB4 kinase.

    Structure. 16, 460-467 (2008)

    PubMed Abstract:  PDB file 3BBW

    Fillgrove KL, Pakhomova S, Schaab M, Newcomer ME, Armstrong RN
    Structure and mechanism of the genomically encoded fosfomycin resistance protein, FosX, from Listeria monocytogenes

    Biochemistry. 46, 8110-8120 (2007)

    PubMed Abstract:  PDB file 2P7K

    Kim SG, Cavalier M, El-Maghrabi MR, Lee YH
    Direct substrate-substrate interaction found in the kinase domain of the bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase

    Journal of Molecular Biology. 370, 14-26 (2007)

    PubMed Abstract:  PDB file 2DWO, 2DWP, and 2I1V

    Vander Kooi CW, Jusino MA, Perman B, Neau DB, Bellamy HD, Leahy DJ
    Structural basis for ligand binding and heparin mediated activation of neuropilin

    Proceedings of the National Academy of Science . 104, 6152-6157 (2007)

    PubMed Abstract:  PDB file 2ORX and 2ORZ

    Sridharan S, Wang L, Dover LG, Brown AK, Kremer L, Besra GS, Sacchettini JC
    X-ray crystal structure of Mycobacterium tuberculosis b-ketoacyl acyl carrier protein synthase II (mtKasB)

    Journal of Molecular Biology. 366, 469-480 (2007)

    PubMed Abstract:  PDB file 2GP6

    Monzingo AF, Ozburn A, Xia S, Meyer RJ, Robertus JD
    The structure of the minimal relaxase domain of MobA at 2.1 Å resolution .

    Journal of Molecular Biology. 366, 165-178 (2007)

    PubMed Abstract:  PDB file 2NS6

    Hindupur A, Liu D, Zhao Y, Bellamy HD, White MA, Fox RO
    The crystal structure of the E. coli stress protein YciF.

    Protein Science. 15, 2605-2611 (2006)

    PubMed Abstract:  PDB file 2GS4

    Russo AT, White MA, Watowich SJ
    The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease.

    Structure. 14, 1449-1458 (2006)

    PubMed Abstract:  PDB file 2HWK

    Bordelon T, Wilkinson SP, Grove A, Newcomer ME
    The crystal structure of the transcriptional regulator HucR from Deinococcus radiourans reveals a repressor preconfigured for DNA binding.

    Journal of Molecular Biology. 360, 168-177 (2006)

    PubMed Abstract; PDB file 2FBK

    Liu L, Song X, He D, Komma C, Kita A, Virbasius JV, Huang G, Bellamy HD, Miki K, Czech MP, Zhou GW
    Crystal Structure of the C2 Domain of Class II Phosphatidylinositide 3-Kinase C2

    Journal of Biological Chemistry. 281, 4254-4260 (2006)

    PubMed Abstract; PDB file 2B3R

    Kim SG, Manes NP, El-Maghrabi R, Lee YH

    Crystal structure of the hypoxia-inducible form of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3): A POSSIBLE NEW TARGET FOR CANCER THERAPY.

    Journal of Biological Chemistry. 281, 2939-2944. (2006)

    PubMed Abstract; PDB file 2AXN

    Vander Kooi CW, Ohi MD, Rosenberg JA, Oldham ML, Newcomer ME, Gould KL, Chazin WJ

    The Prp19 U-box Crystal Structure Suggests a Common Dimeric Architecture for a Class of Oligomeric E3 Ubiquitin Ligases.

    Biochemistry, 45, 121-130 (2006).

    PubMed Abstract; PDB file 2BAY

    Fallon JL, Halling DB, Hamilton SL, Quiocho FA

    Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel.

    Structure (Cambridge). 13, 1881-1886 (2005).

    PubMed Abstract; PDB files 2F3Y and 2F3Z

    Shao H, He X, Achnine L, Blount JW, Dixon RA, Wang X

    Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula.

    Plant Cell, 17, 3141-3154 (2005).

    PubMed Abstract; PDB file 2ACV

    Oldham ML, Brash AR, Newcomer ME

    The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide.

    Proceedings of the National Academy of Science, 102, 297-302 (2005).

    PubMed Abstract; PDB file 1U5U

    Sridharan S, Razvi A, Scholtz JM, Sacchettini JC

    The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers.

    Journal of Molecular Biology, 346, 919-931 (2005).

    PubMed Abstract; PDB file 1Y4Y

    Zhu G, Zhai P, Liu J, Terzyan S, Li G, Zhang XC

    Structural basis of Rab5-Rababtin5 interaction in endocytosis.

    Nature Structural & Molecular Biology, 11, 975-983 (2004).

    PubMed Abstract; PDB file 1TU4

    Zhao Y, Liu D, Kalurachi WD, Bellamy HD, White MA, Fox RO

    The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites.

    Protein Science, 12, 2303-2311 (2003).

    PubMed Abstract; PDB file 1ONS