Akita M, Suzuki A, Kobayashi T, Ito S, Yamane T
Department of Biotechnology and Biomaterial Chemistry, Graduate School of Engineering, Nagoya University, Chikusa-ku, Japan.
Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):749-50. doi: 10.1107/s0907444900003334.
Pel-15, a high-alkaline pectate lyase (pectate transeliminase; E.C. 4.2.2.2) from Bacillus sp. strain KSM-P15, has been crystallized using the hanging-drop vapour-diffusion method at 277 K. Two different crystal forms were obtained and preliminary X-ray diffraction data were collected from each crystal form at 100 K. Both forms belong to the orthorhombic space group P2(1)2(1)2(1) and contain one molecule per asymmetric unit. The unit-cell parameters of form I are a = 43.2 (2), b = 60.2 (2), c = 82.2 (2) A and those of form II are a = 42.9 (1), b = 43.4 (1), c = 105.9 (3) A. Diffraction data to a resolution of 1.5 A were collected from form II crystals using a synchrotron-radiation source.
Pel-15是一种来自芽孢杆菌属菌株KSM-P15的高碱性果胶酸裂解酶（果胶酸反式消除酶；E.C. 4.2.2.2），已采用悬滴气相扩散法于277 K下进行了结晶。获得了两种不同的晶体形式，并在100 K下从每种晶体形式收集了初步的X射线衍射数据。两种形式均属于正交晶系空间群P2(1)2(1)2(1)，每个不对称单元包含一个分子。晶型I的晶胞参数为a = 43.2 (2)，b = 60.2 (2)，c = 82.2 (2) Å，晶型II的晶胞参数为a = 42.9 (1)，b = 43.4 (1)，c = 105.9 (3) Å。使用同步辐射源从晶型II晶体收集了分辨率为1.5 Å的衍射数据。
