Zobrazeno 1 - 10
of 10
pro vyhledávání: '"T. J. Boggon"'
Autor:
John R. Helliwell, D. P. Siddons, Andrzej Olczak, T. J. Boggon, Vivian Stojanoff, Edward H. Snell, R. A. Judge
Publikováno v:
ResearcherID
A comprehensive study of microgravity and ground-grown chicken egg-white lysozyme crystals is presented using synchrotron X-ray reciprocal-space mapping, topography techniques and diffraction resolution. Microgravity crystals displayed reduced intrin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7299d4342f3a308e9b6e7c9660ec500c
https://doi.org/10.1107/s0907444900005837
https://doi.org/10.1107/s0907444900005837
Autor:
D. Peter Siddons, P.F. Zagalsky, T. J. Boggon, Elspeth Gordon, Jun Dong, L. Potthast, Andrew Thompson, Vivian Stojanoff, Naomi E. Chayen, John R. Helliwell, Edward H. Snell, Peter Lautenschlager, Ru–Chang Bi
Publikováno v:
Philosophical Transactions of the Royal Society of London. Series A: Mathematical, Physical and Engineering Sciences. 356:1045-1061
The growth of protein crystals suitable for x-ray crystal structure analysis is an important topic. The quality (perfection) of protein crystals is now being evaluated by mosaicity analysis (rocking curves) and x-ray topographic images as well as the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b05e310313db13d01241701c467151e1
https://doi.org/10.1098/rsta.1998.0208
https://doi.org/10.1098/rsta.1998.0208
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 52:529-533
A Mach-Zehnder interferometer has been developed for the monitoring of the kinetics of the diffusion process in protein crystal growth. This device can be used in conjunction with the ESA Advanced Protein Crystallization Facility (APCF), which allows
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3db3bfdb7f955258ec7370e538806b3b
https://doi.org/10.1107/s090744499600042x
https://doi.org/10.1107/s090744499600042x
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 55:266-268
The subunit C1 of the carotenoid-binding protein, V600, of the chondrophore Velella velella has been purified and crystallized. The crystals, which were grown by the vapour-diffusion method from ammonium sulfate as the major precipitant, diffract bey
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed675b739a92da7385e2f548c8948ed1
https://doi.org/10.1107/s0907444998006908
https://doi.org/10.1107/s0907444998006908
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 59(Pt 7)
Models of apocrustacyanin C(1) were refined against X-ray data recorded on Bending Magnet 14 at the ESRF to resolutions of 1.85 and 2 A from a space-grown and an earth-grown crystal, respectively, both using vapour-diffusion crystal-growth geometry.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abb699bdaa03d6243f188b6f50bdc0f0
https://pubmed.ncbi.nlm.nih.gov/12832753
https://pubmed.ncbi.nlm.nih.gov/12832753
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 55(Pt 4)
A number of methods can be used to improve the stability of the protein crystal-growth environment, including growth in microgravity without an air–liquid phase boundary, growth in gels and growth under oil (`microbatch'). In this study, X-ray data
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dfdb09457123712fec299278effd321
https://pubmed.ncbi.nlm.nih.gov/10089304
https://pubmed.ncbi.nlm.nih.gov/10089304
Autor:
Gordon A. Leonard, Katherine E. McAuley-Hecht, Bernard A. Connolly, R T Walker, E L Hancox, T J Boggon, William N. Hunter, Tom Brown
Publikováno v:
Nucleic acids research. 24(5)
The crystal structure refinement of the synthetic dodecamer d(CGCGAASSCGCG), where S = 4'-thio-2'-deoxythymidine, has converged at R=0.201 for 2605 reflections with F > 2sigma(F) in the resolution range 8.0-2.4 A for a model consisting of the dodecam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99d1ac2ecd54744428d8f9ca5521347e
http://ora.ox.ac.uk/objects/uuid:b82878f4-11c7-4a6c-ad58-0d6c4dc427ec
http://ora.ox.ac.uk/objects/uuid:b82878f4-11c7-4a6c-ad58-0d6c4dc427ec
Autor:
Edgar Weckert, D. P. Siddons, K. Schroer, A. Cassetta, Naomi E. Chayen, Edward H. Snell, K. Hölzer, Vivian Stojanoff, John R. Helliwell, T. J. Boggon
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 52:C517-C517
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d76ef45f769c32a96fecab65ffef89ff
https://doi.org/10.1107/s0108767396078920
https://doi.org/10.1107/s0108767396078920
Autor:
A. Deacon, Naomi E. Chayen, Vivian Stojanoff, T. J. Boggon, S. J. Harrop, T. Ursby, Y.P. Nieh, J. Habash, A. Cassetta, James Raftery, D. P. Siddons, John R. Helliwell, M. R. Peterson, Edward H. Snell, T. Gleichmann, Alfons Hädener, Michael Wulff, Annette C. Niemann, Andrew Thompson
Publikováno v:
Scopus-Elsevier
Macromolecular X-ray crystallography underpins the vigorous field of structural molecular biology having yielded many protein, nucleic acid and virus structures in fine detail. The understanding of the recognition by these macromolecules, as receptor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98934be9041ee4316387b1952866d5f3
http://www.scopus.com/inward/record.url?eid=2-s2.0-10544229793&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-10544229793&partnerID=MN8TOARS
Publikováno v:
ResearcherID
Lysozyme has been crystallized using the ESA Advanced Protein Crystallization Facility onboard the NASA Space Shuttle Orbiter during the IML-2 mission. CCD video monitoring was used to follow the crystallization process and evaluate the growth rate.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33f94d71932a6bc128161c0feba4622a
https://www.ncbi.nlm.nih.gov/pubmed/11540584
https://www.ncbi.nlm.nih.gov/pubmed/11540584