Publication | Open Access
Characterization of two crystal forms of human defensin neutrophil cationic peptide 1, a naturally occurring antimicrobial peptide of leukocytes.
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Citations
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References
1988
Year
ImmunologyMolecular BiologyPeptide SciencePeptide TherapeuticsPeptide ChemistryInflammationProtein FoldingAntimicrobial ResistanceBiochemistryGranulocyteAntimicrobial PeptideCrystal FormsNon-peptide LigandStructural BiologyOrthorhombic Crystal FormsAsymmetric UnitNatural SciencesPeptide LibraryPeptide TherapeuticPeptide SynthesisMicrobiologyMedicine
Two orthorhombic crystal forms (P2(1)2(1)2, a = 30.5 A, b = 44.5 A, c = 40.5 A; I2(1)2(1)2(1) (or I222), a = 30.1 A, b = 66.5 A, c = 35.5 A) of human neutrophil cationic peptide 1 have been characterized. The P2(1)2(1)2 form contains two peptides (Mr = 3425) per asymmetric unit; the I2(1)2(1)2(1) form contains one peptide per asymmetric unit. Both crystal forms diffract to beyond 1.8 A resolution.
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