1ps5: Difference between revisions

Revision as of 12:58, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ps5.png

Template:STRUCTURE 1ps5

STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTIONSTRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 12962625

About this StructureAbout this Structure

1PS5 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Enhancing protein crystallization through precipitant synergy., Majeed S, Ofek G, Belachew A, Huang CC, Zhou T, Kwong PD, Structure. 2003 Sep;11(9):1061-70. PMID:12962625

Page seeded by OCA on Sun Jul 27 12:58:47 2008

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OCA

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-'''STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION'''
+===STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-Suitable conditions for protein crystallization are commonly identified by screening combinations of independent factors that affect crystal formation. Because precipitating agents are prime determinants of crystallization, we investigated whether a systematic exploration of combinations of mechanistically distinct precipitants would enhance crystallization. A crystallization screen containing 64 precipitant mixtures was devised. Tests with ten HIV envelope-related proteins demonstrated that use of precipitant mixtures significantly enhanced both the probability of crystallization as well as the quality of optimized crystals. Tests with hen egg white lysozyme generated a novel C2 crystal from a salt/organic solvent mixture; structure solution at 2 A resolution revealed a lattice held together by both hydrophobic and electrostatic dyad interactions. The results indicate that mechanistically distinct precipitants can synergize, with precipitant combinations adding unique dimensions to protein crystallization.
+The line below this paragraph, {{ABSTRACT_PUBMED_12962625}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12962625}}
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 [[Category: Glycosidase]]
 [[Category: Hydrolase]]
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