193l

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(New page: 200px<br /><applet load="193l" size="450" color="white" frame="true" align="right" spinBox="true" caption="193l, resolution 1.33&Aring;" /> '''THE 1.33 A STRUCTURE...)
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[[Image:193l.gif|left|200px]]<br /><applet load="193l" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:193l.gif|left|200px]]<br /><applet load="193l" size="350" color="white" frame="true" align="right" spinBox="true"
caption="193l, resolution 1.33&Aring;" />
caption="193l, resolution 1.33&Aring;" />
'''THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME'''<br />
'''THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME'''<br />
==Overview==
==Overview==
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Crystals of tetragonal hen egg-white lysozyme were grown using Advanced, Protein Crystallization Facility (APCF) apparatus under a microgravity, environment (SpaceHab-01 mission) and ground control conditions. Crystals, were grown from NaCl as a crystallizing agent at pH 4.3. The X-ray, diffraction patterns of the best diffracting ground- and space-grown, crystals were recorded using synchrotron radiation and an image plate on, the W32 beamline at LURE. Both ground- and space-grown crystals showed, nearly equivalent maximum resolution of 1.3-1.4 A. Refinements were, carried out with the program X-PLOR with final R values of 18.45 and, 18.27% for structures from ground- and space- grown crystals, respectively. The two structures are nearly identical with the, root-mean-square difference on all protein atoms being 0.13 A. Some, residues of the two refined structures show multiple alternative, conformations. Two ions were localized into the electron-density maps of, the two structures: one chloride ion at the interface between two, symmetry-related molecules and one sodium ion stabilizing the loop, Ser60-Leu75. The sodium ion is surrounded by six ligands which form a, bipyramid around it at distances of 2.2-2.6 A.
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Crystals of tetragonal hen egg-white lysozyme were grown using Advanced Protein Crystallization Facility (APCF) apparatus under a microgravity environment (SpaceHab-01 mission) and ground control conditions. Crystals were grown from NaCl as a crystallizing agent at pH 4.3. The X-ray diffraction patterns of the best diffracting ground- and space-grown crystals were recorded using synchrotron radiation and an image plate on the W32 beamline at LURE. Both ground- and space-grown crystals showed nearly equivalent maximum resolution of 1.3-1.4 A. Refinements were carried out with the program X-PLOR with final R values of 18.45 and 18.27% for structures from ground- and space- grown crystals, respectively. The two structures are nearly identical with the root-mean-square difference on all protein atoms being 0.13 A. Some residues of the two refined structures show multiple alternative conformations. Two ions were localized into the electron-density maps of the two structures: one chloride ion at the interface between two symmetry-related molecules and one sodium ion stabilizing the loop Ser60-Leu75. The sodium ion is surrounded by six ligands which form a bipyramid around it at distances of 2.2-2.6 A.
==About this Structure==
==About this Structure==
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193L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CL and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=193L OCA].
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193L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=193L OCA].
==Reference==
==Reference==
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[[Category: Maignan, S.]]
[[Category: Maignan, S.]]
[[Category: Ries-Kautt, M.]]
[[Category: Ries-Kautt, M.]]
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[[Category: Vaney, M.C.]]
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[[Category: Vaney, M C.]]
[[Category: CL]]
[[Category: CL]]
[[Category: NA]]
[[Category: NA]]
[[Category: hydrolase (o-glycosyl)]]
[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:30:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:12 2008''

Revision as of 09:39, 21 February 2008


193l, resolution 1.33Å

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THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME

Overview

Crystals of tetragonal hen egg-white lysozyme were grown using Advanced Protein Crystallization Facility (APCF) apparatus under a microgravity environment (SpaceHab-01 mission) and ground control conditions. Crystals were grown from NaCl as a crystallizing agent at pH 4.3. The X-ray diffraction patterns of the best diffracting ground- and space-grown crystals were recorded using synchrotron radiation and an image plate on the W32 beamline at LURE. Both ground- and space-grown crystals showed nearly equivalent maximum resolution of 1.3-1.4 A. Refinements were carried out with the program X-PLOR with final R values of 18.45 and 18.27% for structures from ground- and space- grown crystals, respectively. The two structures are nearly identical with the root-mean-square difference on all protein atoms being 0.13 A. Some residues of the two refined structures show multiple alternative conformations. Two ions were localized into the electron-density maps of the two structures: one chloride ion at the interface between two symmetry-related molecules and one sodium ion stabilizing the loop Ser60-Leu75. The sodium ion is surrounded by six ligands which form a bipyramid around it at distances of 2.2-2.6 A.

About this Structure

193L is a Single protein structure of sequence from Gallus gallus with and as ligands. Full crystallographic information is available from OCA.

Reference

High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission., Vaney MC, Maignan S, Ries-Kautt M, Ducriux A, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):505-17. PMID:15299672

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