1n4f: Difference between revisions
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'''Para-Arsanilate Derivative of Hen Egg-White Lysozyme''' | {{Structure | ||
|PDB= 1n4f |SIZE=350|CAPTION= <scene name='initialview01'>1n4f</scene>, resolution 1.78Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ASR:4-AMINOPHENYLARSONIC+ACID'>ASR</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | |||
|GENE= | |||
}} | |||
'''Para-Arsanilate Derivative of Hen Egg-White Lysozyme''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1N4F is a [ | 1N4F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4F OCA]. | ||
==Reference== | ==Reference== | ||
Phasing power at the K absorption edge of organic arsenic., Retailleau P, Prange T, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):887-96. Epub 2003, Apr 25. PMID:[http:// | Phasing power at the K absorption edge of organic arsenic., Retailleau P, Prange T, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):887-96. Epub 2003, Apr 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12777806 12777806] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:02 2008'' | ||
Revision as of 13:52, 20 March 2008
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| , resolution 1.78Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Para-Arsanilate Derivative of Hen Egg-White Lysozyme
OverviewOverview
Single/multiple-wavelength anomalous dispersion (SAD/MAD) experiments were performed on a crystal of an organic arsenic derivative of hen egg-white lysozyme. A para-arsanilate compound used as a crystallizing reagent was incorporated into the ordered solvent region of the lysozyme molecule. Diffraction data were collected to high resolution (</=2.0 A) at three wavelengths around the K edge (1.04 A) of arsenic at beamline BM30A, ESRF synchrotron. Anomalous Patterson maps clearly showed the main arsanilate site to be between three symmetry-related lysozyme molecules, at a location previously occupied by a para-toluenesulfonate anion. MAD phases at 2 A derived using the program SHARP led to an electron-density map of sufficient quality to start manual building of the protein model. Amplitudes from a second crystal measured to a resolution of 1.8 A at the peak wavelength revealed two additional heavy-atom sites, which reinforced the anomalous subset model and therefore dramatically improved the phasing power of the arsenic derivative. The subsequent solvent-flattened map was of such high accuracy that the program ARP/wARP was able to build a nearly complete model automatically. This work emphasizes the great potential of arsenic for de novo structure determination using anomalous dispersion methods.
About this StructureAbout this Structure
1N4F is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
Phasing power at the K absorption edge of organic arsenic., Retailleau P, Prange T, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):887-96. Epub 2003, Apr 25. PMID:12777806
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