1bhz

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[[Image:1bhz.gif|left|200px]]
[[Image:1bhz.gif|left|200px]]
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{{Structure
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|PDB= 1bhz |SIZE=350|CAPTION= <scene name='initialview01'>1bhz</scene>, resolution 3.9&Aring;
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bhz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhz OCA], [http://www.ebi.ac.uk/pdbsum/1bhz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bhz RCSB]</span>
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'''LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE LYSOZYME FROM MASC DATA'''
'''LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE LYSOZYME FROM MASC DATA'''
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[[Category: Ramin, M.]]
[[Category: Ramin, M.]]
[[Category: Shepard, W.]]
[[Category: Shepard, W.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: masc]]
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[[Category: Masc]]
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[[Category: multiwavelength anomalous solvent contrast]]
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[[Category: Multiwavelength anomalous solvent contrast]]
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[[Category: o-glycosyl]]
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[[Category: O-glycosyl]]
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Revision as of 08:32, 2 May 2008

Template:STRUCTURE 1bhz

LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE LYSOZYME FROM MASC DATA


Overview

A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48] presented the theoretical foundations of MASC, a new contrast-variation method using multiwavelength anomalous scattering, and reported the first experimental results. New experiments have been conducted both at the ESRF (Grenoble, France) and at LURE-DCI (Orsay, France), using cryocooled crystals of three proteins of known structures and very different molecular weights. Amplitudes of {GammaT(h)}, the 'normal' structure factors of the anomalously scattering part of the crystal including the solvent zone and the ordered anomalous scattering sites (if any), have been extracted from multiwavelength data. In the very low resolution range (d >/= 20 A), the agreement between experimental {GammaT(h)} and model values calculated from the bulk solvent is all the more satisfactory since the molecular weight of the protein is high. For spacings between 10 and 20 A, the agreement between experimental {GammaT(h)} and model values is also satisfactory if one takes into account ordered anomalous scatterer sites. Such sites have been found in the three cases.

About this Structure

1BHZ is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values., Ramin M, Shepard W, Fourme R, Kahn R, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):157-67. Epub 1999, Jan 1. PMID:10089406 Page seeded by OCA on Fri May 2 11:32:16 2008

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