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151l

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[[Image:151l.gif|left|200px]]
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[[Image:151l.png|left|200px]]
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{{STRUCTURE_151l| PDB=151l | SCENE= }}
{{STRUCTURE_151l| PDB=151l | SCENE= }}
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'''CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME'''
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===CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME===
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==Overview==
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Solvent-binding sites were compared in 10 different crystal forms of phage T4 lysozyme that were refined using data from 2.6 A to 1.7 A resolution. The sample included 18 crystallographically independent lysozyme molecules. Despite different crystallization conditions, variable crystal contacts, changes due to mutation, and varying attention to solvent during crystallographic refinement, 62% of the 20 most frequently occupied sites were conserved. Allowing for potential steric interference from neighboring molecules in the crystal lattice, this fraction increased to 79% of the sites. There was, however, no solvent-binding site that was occupied in all 18 lysozyme molecules. A buried double site was occupied in 17 instances and 2 other internal sites were occupied 15 times. Apart from these buried sites, the most frequently occupied sites were often at the amino-termini of alpha-helices. Solvent molecules at the most conserved sites tended to have crystallographic thermal factors lower than average, but atoms with low B-factors were not restricted to these sites. Although superficial inspection may suggest that only 50-60% (or less) of solvent-binding sites are conserved in different crystal forms of a protein, it appears that many sites appear to be empty either because of steric interference or because the apparent occupancy of a given site can vary from crystal to crystal. The X-ray method of identifying sites is somewhat subjective and tends to result in specification only of those solvent molecules that are well ordered and bound with high occupancy, even though there is clear evidence for solvent bound at many additional sites.(ABSTRACT TRUNCATED AT 250 WORDS)
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(as it appears on PubMed at http://www.pubmed.gov), where 7920248 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7920248}}
==About this Structure==
==About this Structure==
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[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Zhang, X J.]]
[[Category: Zhang, X J.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:30:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:31:15 2008''

Revision as of 12:31, 30 June 2008

Image:151l.png

Template:STRUCTURE 151l

CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME

Template:ABSTRACT PUBMED 7920248

About this Structure

151L is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme., Zhang XJ, Matthews BW, Protein Sci. 1994 Jul;3(7):1031-9. PMID:7920248

Page seeded by OCA on Mon Jun 30 15:31:15 2008

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