1bhy
From Proteopedia
(New page: 200px<br /><applet load="1bhy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bhy, resolution 4.18Å" /> '''LOW TEMPERATURE MIDD...) |
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| - | [[Image:1bhy.gif|left|200px]]<br /><applet load="1bhy" size=" | + | [[Image:1bhy.gif|left|200px]]<br /><applet load="1bhy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bhy, resolution 4.18Å" /> | caption="1bhy, resolution 4.18Å" /> | ||
'''LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF P64K FROM MASC DATA'''<br /> | '''LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF P64K FROM MASC DATA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48] | + | 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== | ==About this Structure== | ||
| - | 1BHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1BHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: outer membrane protein]] | [[Category: outer membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:27 2008'' |
Revision as of 09:55, 21 February 2008
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LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF P64K 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
1BHY is a Single protein structure of sequence from Neisseria meningitidis with as ligand. 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
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