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Lehmann, M. S., Pebay-Peyroula, E. (1992) Location of the sulfur atoms from the phased anomalous map using native protein data can be very helpful in tracing the peptide chain. Acta Crystallographica Section B Structural Science, 48 (1) 115-116 doi:10.1107/s0108768191011011

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Reference TypeJournal (article/letter/editorial)
TitleLocation of the sulfur atoms from the phased anomalous map using native protein data can be very helpful in tracing the peptide chain
JournalActa Crystallographica Section B Structural Science
AuthorsLehmann, M. S.Author
Pebay-Peyroula, E.Author
Year1992 (February 1)Volume48
Issue1
PublisherInternational Union of Crystallography (IUCr)
DOIdoi:10.1107/s0108768191011011Search in ResearchGate
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Mindat Ref. ID189792Long-form Identifiermindat:1:5:189792:4
GUID0
Full ReferenceLehmann, M. S., Pebay-Peyroula, E. (1992) Location of the sulfur atoms from the phased anomalous map using native protein data can be very helpful in tracing the peptide chain. Acta Crystallographica Section B Structural Science, 48 (1) 115-116 doi:10.1107/s0108768191011011
Plain TextLehmann, M. S., Pebay-Peyroula, E. (1992) Location of the sulfur atoms from the phased anomalous map using native protein data can be very helpful in tracing the peptide chain. Acta Crystallographica Section B Structural Science, 48 (1) 115-116 doi:10.1107/s0108768191011011
In(1992, February) Acta Crystallographica Section B Structural Science Vol. 48 (1) International Union of Crystallography (IUCr)

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Timmins, P. A., Pebay-Peyroula, E., Penel, S. (1996) Detergent localization in membrane protein crystals using neutron diffraction. Acta Crystallographica Section A Foundations of Crystallography, 52. doi:10.1107/s0108767396093622
Sheriff, S., Hendrickson, W. A. (1987) Location of iron and sulfur atoms in myohemerythrin from anomalous-scattering measurements. Acta Crystallographica Section B Structural Science, 43 (2) 209-212 doi:10.1107/s0108768187098057
Edman, K., Royant, A., Nollert, P., Navarro, J., Pebay-Peyroula, E., Landau, E. M., Neutze, R. (2002) Early structural rearrangements in the photocycles of bacteriorhodopsin and sensory rhodopsin II. Acta Crystallographica Section A Foundations of Crystallography, 58. doi:10.1107/s0108767302093340
Panwar, Pankaj, Deniaud, Aurélien, Pebay-Peyroula, Eva (2012) Contamination from an affinity column: an encounter with a new villain in the world of membrane-protein crystallization. Acta Crystallographica Section D Biological Crystallography, 68 (10). 1272-1277 doi:10.1107/s090744491202639x
Klooster, W. T., Swaminathan, S., Nanni, R., Craven, B. M. (1992) Electrostatic properties of 1-methyluracil from diffraction data. Acta Crystallographica Section B Structural Science, 48 (2) 217-227 doi:10.1107/s0108768191013319
Vegas, A., MartĂ­nez-Ripoll, M. (1992) From crystal structure data towards reaction paths in the solid state?. Acta Crystallographica Section B Structural Science, 48 (6) 747-752 doi:10.1107/s0108768192004324
Vachette, P., Durand, D., Raibaud, S., Dardel, F., Dubosclard, V., Fieschi, F., Pebay-Peyroula, E. (2005) Structural biology studies coupling SAXS with crystallography and NMR. Acta Crystallographica Section A Foundations of Crystallography, 61. doi:10.1107/s0108767305095498
Edman, K., Nollert, P., Royant, A., Belrhali, H., Pebay-Peyroula, E., Ursby, T., Hajdu, J., Neutze, R., Landau, E. M. (2000) Portrait of a membrane protein in action: bacterio-rhodopsin pumping protons. Acta Crystallographica Section A Foundations of Crystallography, 56. doi:10.1107/s0108767300025666
Dahout-Gonzalez, CĂ©cile, Brandolin, GĂ©rard, Pebay-Peyroula, Eva (2003) Crystallization of the bovine ADP/ATP carrier is critically dependent upon the detergent-to-protein ratio. Acta Crystallographica Section D Biological Crystallography, 59 (12). 2353-2355 doi:10.1107/s0907444903020699
IUCr, (1992) New Section of Acta Crystallographica. Acta Crystallographica Section B Structural Science, 48 (2) 117 doi:10.1107/s0108768192099828
Grizot, S., Fauré, J., Fieschi, F., Vignais, P., Dagher, M.-C., Pebay-Peyroula, E. (2000) Structure of the complex between Rac1 and its inhibitor partner RhoGDI at 2.7 Å resolution. Acta Crystallographica Section A Foundations of Crystallography, 56. doi:10.1107/s0108767300026155
 
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