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Structure paper

TitleUse of differentially substituted selenomethionine proteins in X-ray structure determination.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 55, Page 1967-1970, Year 1999
Publish dateAug 28, 1999 (structure data deposition date)
AuthorsGassner, N.C. / Matthews, B.W.
External linksActa Crystallogr. ,Sect. D / PubMed:10666571
MethodsX-ray diffraction
Resolution1.89 - 2.12 Å
Structure data

PDB-1cx7:
T4 LYSOZYME METHIONINE CORE MUTANT
Method: X-RAY DIFFRACTION / Resolution: 1.94 Å

PDB-1d2w:
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

PDB-1d2y:
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
Method: X-RAY DIFFRACTION / Resolution: 2.06 Å

PDB-1d3f:
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-1d3j:
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

PDB-1d3m:
METHIONINE CORE MUTATION
Method: X-RAY DIFFRACTION / Resolution: 2.12 Å

PDB-1d3n:
METHIONINE CORE MUTATION
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-HED:
2-HYDROXYETHYL DISULFIDE

ChemComp-HOH:
WATER

Source
  • enterobacteria phage t4 (virus)
KeywordsHYDROLASE / HYDROLASE (O-GLYCOSYL) / T4 LYSOZYME / METHIONINE CORE MUTANT / PROTEIN ENGINEERING / PROTEIN FOLDING / SELENOMETHIONINE

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