The F(1) part of the F(1)F(O) ATP synthase from Escherichia coli has been crystallized and its structure determined to 4.4-A resolution by using molecular replacement based on the structure of the beef-heart mitochondrial enzyme. The bacterial F(1) consists of five subunits with stoichiometry alpha(3), beta(3), gamma, delta, and epsilon. delta was removed before crystallization. In agreement wi...

Protein L consists of a single alpha-helix packed on a four-stranded beta-sheet formed by two symmetrically opposed beta-hairpins. We use a computer-based protein design procedure to stabilize a domain-swapped dimer of protein L in which the second beta-turn straightens and the C-terminal strand inserts into the beta-sheet of the partner. The designed obligate dimer contains three mutations (A5...

The intensities of a sufficient number of X-ray diffraction maxima determine the structure of a crystal, that is, the positions of the atoms in the unit cell of the crystal. The available intensities usually exceed the number of parameters needed to describe the structure. From these intensities a set of numbers jEHj can be derived, one corresponding to each intensity. However, the elucidation ...

It is demonstrated that standard in-house protein crystal X-ray diffraction apparatus can be used to measure very low resolution reflections with only a few modifications. The apparatus and modifications are described in detail and tested on two different macromolecular crystal samples: lysozyme and the 30S ribosomal subunit. Contrast-variation measurements on tetragonal hen egg-white lysozyme ...

The structure of the octameric histone core of the nucleosome has been determined by x-ray crystallography to a resolution of 3.1 A. The histone octamer is a tripartite assembly in which a centrally located (H3-H4)2 tetramer is flanked by two H2A-H2B dimers. It has a complex outer surface; depending on the perspective, the structure appears as a wedge or as a flat disk. The disk represents the ...

Finding the structure of proteins and protein-protein complexes is an important problem in the field of computational biology. Determining protein structures can be done successfully with various experimental methods like x-ray crystallography, but determining protein-protein structures experimentally is more difficult. Instead, these structures are frequently predicted computationally. One app...

In this article, we report a method for coarse-grained normal mode analysis called the minimalist network model. The main features of the method are that it can deliver accurate low-frequency modes on structures without undergoing initial energy minimization and that it also retains the details of molecular interactions. The method does not require any additional adjustable parameters after coa...

To celebrate a century of X-ray crystallography, I describe how 100 crystal structures influenced chromatin and transcription research.

A bis-urea macrocycle 1 was synthesized and shown to form extended nanotubular columns by X-ray crystallography.