Bento I, Frazão C, Coelho R, Wilson K, Dauter Z, Carrondo M A
Instituto de Tecnologia Química e Biológica, Apartado 127, 2780-Oeiras, Portugal.
Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):991-3. doi: 10.1107/s0907444998001048.
The plant aspartic proteinase cardosin A was crystallized using vapour diffusion. Crystals belong to the monoclinic space group C2, cell dimensions a = 116.9 (2), b = 87.2 (8), c = 81.3 (1) A, beta = 104.4 (4) degrees, and contain two molecules in the asymmetric unit related by a non-crystallographic twofold axis. Diffraction data were collected at room temperature with radiation from a synchrotron source up to 2.85 A resolution. When the crystals were flash cooled to 110 K in a nitrogen stream the same resolution limit could also be obtained on a rotating-anode source. Recently, synchrotron radiation together with flash cooling led to an improvement of the diffraction data to 1.72 A resolution.
植物天冬氨酸蛋白酶卡多辛A通过气相扩散法结晶。晶体属于单斜空间群C2，晶胞参数a = 116.9 (2)、b = 87.2 (8)、c = 81.3 (1) Å，β = 104.4 (4)°，不对称单元中含有两个通过非晶体学二重轴相关的分子。在室温下用同步辐射源收集衍射数据，分辨率达到2.85 Å。当晶体在氮气流中快速冷却至110 K时，在旋转阳极源上也能获得相同的分辨率极限。最近，同步辐射与快速冷却相结合使衍射数据的分辨率提高到了1.72 Å。
