DATA COLLECTION ON RIBOSOMAL PROTEIN S15 & RRNA COMPLEX

细菌核糖体的结构研究一直是有限的 低分辨率低温电子显微镜和X射线 整个核糖体的衍射研究，或高分辨率X射线 和核磁共振研究单个核糖体蛋白。 我们有 成功地共结晶了芽孢杆菌核糖体蛋白S15 嗜热脂肪菌的核糖体RNA结合位点。 这些 然而，晶体不会生长得比0.6 × 0.2 × 0.2 mm大得多， 在室内低温条件下，对3.5 E有微弱作用。 这项工作 需要同步辐射来收集天然晶体的数据， 尽可能高的分辨率，并收集潜在的数据， 同晶重原子衍生物晶体。

Structural studies of the bacterial ribosome have been limited either to low resolution cryo-electron microscopy and x-ray diffraction studies of whole ribosomes, or to high resolution x-ray and NMR studies of individual ribosomal proteins. We have successfully co-crystallized the ribosomal protein S15 from Bacillus stearothermophilus with its ribosomal RNA binding site. These crystals, however, do not grow much larger than 0.6 x 0.2 x 0.2 mm and diffract weakly to 3.5 E in house under cryo conditions. This work requires synchrotron radiation to collect data on native crystals to the highest possible resolution and to collect data on potential isomorphous heavy atom derivative crystals.