Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability (Q27640747)

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scientific article (publication date: April 2003)

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English	Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability	scientific article (publication date: April 2003)

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scholarly article

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title

Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability (English)

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author name string

Mats Sandgren

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1

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Peter J Gualfetti

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2

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Andrew Shaw

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3

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Laurie S Gross

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4

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Mae Saldajeno

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5

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Anthony G Day

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6

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T Alwyn Jones

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7

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Colin Mitchinson

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8

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publication date

April 2003

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published in

Protein Science

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volume

12

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issue

4

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page(s)

848-60

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cites work

The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 A resolution

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The X-ray crystal structure of the Trichoderma reesei family 12 endoglucanase 3, Cel12A, at 1.9 A resolution

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The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution

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The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution

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Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive

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Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3

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Solvent content of protein crystals

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Two exposed amino acid residues confer thermostability on a cold shock protein

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Identifiers

DOI

10.1110/PS.0237703

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PMC publication ID

2323842

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PubMed publication ID

12649442

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ResearchGate publication ID

230553647

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