Abstract
A hexagonal crystal form ( P6 322, a = b = 34.0 A ̊ , c = 113.5 A ̊ ) and a monoclinic form ( P2 1, a = 37.1 A ̊ , b = 32.2 A ̊ , c = 32.4 A ̊ , β = 110 ° ) of neutrophil cationic protein NP2, isolated from rabbit leukocytes, have been characterized. The monoclinic form, containing two promoters ( M r = 3844) per asymmetric unit, diffracts to at least 1.8 Å and is suitable for high-resolution structural studies.
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