Crystallization and preliminary X‐ray analysis of the ternary complex of procarboxypeptidase A from bovine pancreas

FEBS Letters

Ventura, S.¹  Gómez, M.¹  Gomis-Rüth, F.X.¹  Avilés, F.X.¹  Vendrell, J.¹ 

[1] Institut de Biologia Fonamental i Departament de Bioquimica i de Biologia Molecular, Facultat de Ciències, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain

关键词: Protein crystallization;    X-Ray crystallography;    Ternary complex;    Procarboxypeptidase A;    Chymotrypsinogen C;    Proproteinase E;    V m;    Matthews-parameter (protein volume per mass unit in the crystal);    TC;    ternary complex;    PCPA;    procarboxypeptidase A;    CTGC;    chymotrypsinogen C;    BPE;    proproteinase E;    FPLC;    fast performance liquid chromatography;    PEG;    polyethylenglycol;   

DOI  :  10.1016/0014-5793(95)00533-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ternary complex of procarboxypeptidase A, chymotrypsinogen C and proproteinase E from bovine pancreas has been crystallized using the sitting drop vapour diffusion method. The success in obtaining crystals has been found to be critically dependent on the prevention of autolysis of the complex. In preliminary stages, crystals twinned by merohedry were obtained from a solution containing MgCl₂ and polyethylenglycol 400 as precipitating agent. Later on, untwinned ones could be grown employing CaCl₂ instead of MgCl₂. These latter crystals belong to the rhombohedral system and to the spacegroup R3 with cell dimensions . Consideration of the possible values of V _m accounts for the presence of one ternary complex molecule-oligomere per asymmetric unit. The crystals diffract beyond 2.6 Å resolution and are suitable for X-ray analysis.

【 授权许可】

Unknown