1ps5: Difference between revisions

Revision as of 15:32, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1PS5 is a Single protein structure of sequence from Gallus gallus with as ligand. Active as Lysozyme, with EC number 3.2.1.17 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 Thu Feb 21 14:31:59 2008

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OCA

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-[[Image:1ps5.jpg|left|200px]]<br /><applet load="1ps5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ps5.jpg|left|200px]]<br /><applet load="1ps5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ps5, resolution 2.00&Aring;" />
 '''STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION'''<br />
 ==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.
+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.
 ==About this Structure==
-PS5 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PS5 OCA].
+PS5 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PS5 OCA].
 ==Reference==
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 [[Category: Belachew, A.]]
 [[Category: Huang, C.]]
-[[Category: Kwong, P.D.]]
+[[Category: Kwong, P D.]]
 [[Category: Majeed, S.]]
 [[Category: Ofek, G.]]
@@ Line 24: / Line 24: @@
 [[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:04:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:59 2008''