Human plasminogen kringle 4. Crystallization and preliminary diffraction data of two different crystal forms.
Human plasminogen kringle 4 has been crystallized in two different crystal forms: monoclinic, a = 32.78(3), b = 49.17(2), c = 46.27(3) A, beta = 100.67 degrees, space group P2(1), four molecules/unit cell, two molecules/asymmetric unit; orthorhombic, a = 32.09(7), b = 49.14(6), c = 49.47(9) A, space group P2(1)2(1)2, four molecules/unit cell. Both crystal forms have a large protein fraction (66% for monoclinic and 62% for orthorhombic) and diffract x-rays to 2.0 A resolution. A self-rotation function has been calculated with monoclinic data indicating a non-crystallographic 2-fold rotation approximately parallel to a* (peak height of 14.3 x sigma). Cross-rotation function calculations are in progress utilizing the coordinates of the conserved structure of kringle 1 of prothrombin and plasminogen kringle 4.
Mulichak
A M
AM
Department of Chemistry, Michigan State University, East Lansing 48824.
Park
C H
CH
Tulinsky
A
A
Petros
A M
AM
Llinás
M
M
D003460:Crystallization; D006801:Humans; D010196:Pancreatic Elastase; D010446:Peptide Fragments / Q000302:isolation & purification; D010958:Plasminogen / Q000302:isolation & purification; D011487:Protein Conformation; D014961:X-Ray Diffraction
D010446:Peptide Fragments; D010958:Plasminogen; D010196:Pancreatic Elastase