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Structure paper

TitleProtein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 57, Page 679-688, Year 2001
Publish dateSep 11, 2000 (structure data deposition date)
AuthorsLongenecker, K.L. / Garrard, S.M. / Sheffield, P.J. / Derewenda, Z.S.
External linksActa Crystallogr. ,Sect. D / PubMed:11320308
MethodsX-ray diffraction
Resolution2 - 2.8 Å
Structure data

PDB-1fso:
CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI QUADRUPLE MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1fst:
CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI TRIPLE MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-1ft0:
CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-1ft3:
CRYSTAL STRUCTURE OF TRUNCATED RHOGDI K141A MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN INHIBITOR / immunoglobulin fold / beta sandwich motif / isoprenyl-binding domain / GDP-dissociation inhibitor of Rho GTPases

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