1n4f
From Proteopedia
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Para-Arsanilate Derivative of Hen Egg-White Lysozyme
Overview
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 Structure
1N4F is a Single protein structure of sequence from Gallus gallus with NA, ASR and EDO as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
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:12777806
Page seeded by OCA on Tue Nov 20 21:57:13 2007
Categories: Gallus gallus | Lysozyme | Single protein | Prange, T. | Retailleau, P. | ASR | EDO | NA | Hydrolase
