CRYSTALLOGRAPHIC STUDY OF HUMAN RECOMBINANT FACTOR XIII

我们已经使用以下方法改进了因子XIII酶原的晶体结构： 在SSRL收集的衍射数据。 有两种模式 活化：在低Ca 2+和高Ca 2+存在下凝血酶裂解 钙浓度 我们随后确定了 凝血酶裂解因子XIII和非裂解因子的结构 XIII在高浓度钙和钙的存在下 类似物 在这两种形式中，分子的活性部位 仍然受阻。 继续工作的重点是结构 活性因子XIII及其与底物类似物复合物研究 和抑制剂。 为了达到这个目的，我们已经成长为弱衍射 抑制因子XIII的晶体。

We have refined the crystal structure of factor XIII zymogen using diffraction data collected at SSRL. There are two modes of activation: thrombin cleavage in the presence of low Ca2+, and high calcium concentration. We have subsequently determined the crystal structures of thrombin-cleaved factor XIII and of non-cleaved factor XIII in the presence of high concentrations of calcium and calcium analogues. In both these forms, the active site of the molecule remains obstructed. Continuing work is focused on the structural study of active factor XIII and its complexes with substrate analogues and inhibitors. Toward that end, we have grown weakly diffracting crystals of inhibited factor XIII.