Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs.

The X-ray structure of the homotetrameric lysosomal acid hydrolase, human beta-glucuronidase (332,000 Mr), has been determined at 2.6 A resolution. The tetramer has approximate dihedral symmetry and each promoter consists of three structural domains with topologies similar to a jelly roll barrel, an immunoglobulin constant domain and a TIM barrel respectively.

Forced coalescence phasing: a method for ab initio determination of crystallographic phases.

A method has been developed for ab initio determination of crystallographic phases. This technique, called forced coalescence phasing (FCP), is implemented on a computer and uses an automated iterative procedure that combines real space filtering with numerically seeded Fourier transforms to solve the crystallographic phase problem. This approach is fundamentally different from that of traditional direct methods of phasing, which rely on structure invariant probabilistic phase relationships.

Crystallization and preliminary crystallographic studies of human beta-glucuronidase.

Crystals of human beta-glucuronidase have been obtained by the vapor diffusion method, using 2-methyl-2,4-pentanediol as a precipitant. The crystals belong to the orthorhombic space group P222(1), with cell dimensions a = 134.5 A, b = 95.

A highly propeller-twisted adenine-adenine base pair in 8-tert-butyladenine.

C9H13N5, Mr = 191.24, monoclinic, P2(1)/c, a = 7.562 (1), b = 6.

Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution.

The structure of troponin C has been refined at 2A resolution to an R value of 0.172 using a total of 8,100 reflections. Troponin C has an unusual dumbbell shape with only the two C-domain high affinity sites III and IV occupied with metals, while the pair of N-domain low affinity sites I and II are devoid of metals.