Gruez A, Zeghouf M, Bertrand J, Eschenbrenner M, Covès J, Fontecave M, Pignol D, Fontecilla-Camps J C
Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale J. P. Ebel, CEA-CNRS, 41 avenue de Martyrs, 38027 Grenoble CEDEX 1, France.
Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):135-6. doi: 10.1107/s090744499701069x.
The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein subunit was crystallized using the hanging-drop technique, with PEG 4000 as precipitant. The crystals belong to space group P3112 or enantiomorph, with unit-cell parameters a = b = 171.0, c = 152.1 A. A solvent content of 75% was determined by a calibrated tetrachloromethane/toluene gradient which corresponds to three monomers per asymmetric unit. A 3 A resolution native data set was collected at beamline W32 of LURE, Orsay, France.
利用悬滴法，以聚乙二醇4000作为沉淀剂，使大肠杆菌亚硫酸盐还原酶黄素蛋白亚基的FNR样结构域结晶。晶体属于P3112空间群或对映体，晶胞参数a = b = 171.0，c = 152.1 Å。通过校准的四氯甲烷/甲苯梯度测定溶剂含量为75%，这对应于每个不对称单元有三个单体。在法国奥赛LURE的W32光束线收集了分辨率为3 Å的天然数据集。
