1uo6: Difference between revisions
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==Overview== | ==Overview== | ||
Complete and highly redundant data sets were collected at nine different, wavelengths between 0.80 and 2.65 A on a xenon derivative of porcine, pancreatic elastase in both air and helium atmospheres. The magnitude of, the anomalous signal, as assessed by the xenon-peak height in the, anomalous difference Patterson synthesis, is affected by the wavelength of, data collection as well as by the scaling model used. For data collected, at wavelengths longer than 1.7 A, the use of a three-dimensional scaling, protocol is essential in order to obtain the highest possible anomalous, signal. Based on the scaling protocols currently available, the optimal, wavelength range for data collection appears to be between 2.1 and 2.4 A., Beyond that, any further increase in signal will be compensated for . | Complete and highly redundant data sets were collected at nine different, wavelengths between 0.80 and 2.65 A on a xenon derivative of porcine, pancreatic elastase in both air and helium atmospheres. The magnitude of, the anomalous signal, as assessed by the xenon-peak height in the, anomalous difference Patterson synthesis, is affected by the wavelength of, data collection as well as by the scaling model used. For data collected, at wavelengths longer than 1.7 A, the use of a three-dimensional scaling, protocol is essential in order to obtain the highest possible anomalous, signal. Based on the scaling protocols currently available, the optimal, wavelength range for data collection appears to be between 2.1 and 2.4 A., Beyond that, any further increase in signal will be compensated for or, even superseded by a concomitant increase in noise, which cannot be fully, corrected for. Data collection in a helium atmosphere yields higher, I/sigma(I) values, but not significantly better anomalous differences, than data collection in air. | ||
==About this Structure== | ==About this Structure== | ||
1UO6 is a | 1UO6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with SO4, CL, NA, XE and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UO6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: xenon binding]] | [[Category: xenon binding]] | ||
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Revision as of 14:28, 5 November 2007
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PORCINE PANCREATIC ELASTASE/XE-COMPLEX
OverviewOverview
Complete and highly redundant data sets were collected at nine different, wavelengths between 0.80 and 2.65 A on a xenon derivative of porcine, pancreatic elastase in both air and helium atmospheres. The magnitude of, the anomalous signal, as assessed by the xenon-peak height in the, anomalous difference Patterson synthesis, is affected by the wavelength of, data collection as well as by the scaling model used. For data collected, at wavelengths longer than 1.7 A, the use of a three-dimensional scaling, protocol is essential in order to obtain the highest possible anomalous, signal. Based on the scaling protocols currently available, the optimal, wavelength range for data collection appears to be between 2.1 and 2.4 A., Beyond that, any further increase in signal will be compensated for or, even superseded by a concomitant increase in noise, which cannot be fully, corrected for. Data collection in a helium atmosphere yields higher, I/sigma(I) values, but not significantly better anomalous differences, than data collection in air.
About this StructureAbout this Structure
1UO6 is a Single protein structure of sequence from Sus scrofa with SO4, CL, NA, XE and GOL as ligands. Active as Pancreatic elastase, with EC number 3.4.21.36 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
On the routine use of soft X-rays in macromolecular crystallography. Part II. Data-collection wavelength and scaling models., Mueller-Dieckmann C, Polentarutti M, Djinovic Carugo K, Panjikar S, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):28-38. Epub 2003, Dec 18. PMID:14684889
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