| Structural highlights
1uo6 is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , |
| Related: | 1b0e, 1bma, 1btu, 1c1m, 1e34, 1e35, 1e36, 1e37, 1e38, 1eai, 1eas, 1eat, 1eau, 1ela, 1elb, 1elc, 1eld, 1ele, 1elf, 1elg, 1esa, 1esb, 1est, 1fle, 1fzz, 1gvk, 1gwa, 1h9l, 1hax, 1hay, 1haz, 1hb0, 1hv7, 1inc, 1jim, 1l0z, 1l1g, 1lka, 1lkb, 1lvy, 1mcv, 1mmj, 1nes, 1okx, 1qgf, 1qix, 1qnj, 1qr3, 2est, 3est, 4est, 5est, 6est, 7est, 8est, 9est |
| Activity: | Pancreatic elastase, with EC number 3.4.21.36 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[CELA1_PIG] Acts upon elastin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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appears to be between 2.1 and 2.4 A. Beyond that, any further increase in signal will be compensated for or even superseded by a concomitant increase in noise, which cannot be fully corrected for.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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mueller-Dieckmann C, Polentarutti M, Djinovic Carugo K, Panjikar S, Tucker PA, Weiss MS. On the routine use of soft X-rays in macromolecular crystallography. Part II. Data-collection wavelength and scaling models. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):28-38. Epub 2003, Dec 18. PMID:14684889
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