scispace - formally typeset
R

Robert Huber

Researcher at Technische Universität München

Publications -  742
Citations -  76282

Robert Huber is an academic researcher from Technische Universität München. The author has contributed to research in topics: Active site & Protein structure. The author has an hindex of 139, co-authored 671 publications receiving 73557 citations. Previous affiliations of Robert Huber include Munich University of Applied Sciences & Russian Academy of Sciences.

Papers
More filters
Journal ArticleDOI

Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement

TL;DR: In this article, a statistical survey of X-ray structures of small compounds from the Cambridge Structural Database is used for the refinement of protein structures determined by X-Ray crystallography.
Journal ArticleDOI

Structure of 20S proteasome from yeast at 2.4 A resolution.

TL;DR: Two β-type subunits are processed to an intermediate form, indicating that an additional nonspecific endopeptidase activity may exist which is important for peptide hydrolysis and for the generation of ligands for class I molecules of the major histocompatibility complex.
Journal ArticleDOI

X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis

TL;DR: In this paper, an atomic model of the prosthetic groups of the reaction center complex (4 bacteriochlorophyll b, 2 bacteriopheophytin b, 1 non-heme iron, 1 menaquinone, 4 heme groups) was built.
Journal ArticleDOI

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.

TL;DR: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging.
Journal ArticleDOI

The complete genome of the hyperthermophilic bacterium Aquifex aeolicus

TL;DR: The complete genome sequence of A. aeolicus is described, consisting of 1,551,335 base pairs, and it is shown that the use of oxygen (albeit at very low concentrations) as an electron acceptor is allowed by the presence of a complex respiratory apparatus.