While working on the crystal structure of the 250-kDa Ca2+-calmodulin-dependent kinase II (CaMKII) core in John Kuryans laboratory, André developed a strong fascination for macromolecular assemblies. Inspired by the large CaMKII structure, André joined Günter Blobels laboratory with the idea of starting a comprehensive structural and functional characterization of the ~120 million Dalton nuclear pore complex (NPC), one of the largest proteinaceous assemblies in eukaryotic cells. In Günter Blobels laboratory André set up a structural biology subgroup that established the NPC as a viable target for an interdisciplinary divide-and-conquer approach, employing X-ray crystallographic, biochemical and in vivo studies, funded by a grant from the Leukemia and Lymphoma Society. Simultaneously, André stared a second line of research on the regulation of the histone-modifying machinery. André joined the Caltech faculty in November 2010.
The Hoelz lab carries out structure-function studies of the nuclear pore complex with the ultimate goal of elucidating the atomic structure of the NPC. The applied structure determination as well as the described design principles of the NPC may serve as paradigms for other macromolecular assemblies.
Ch 10 abc. Frontiers in Chemistry.1 unit (1-0-0) first, second terms; 6 units (1-4-1) third term.; first, second, third terms, 2022-23.Prerequisites: Open for credit to first-year students and sophomores. Ch 10 c prerequisites are Ch 10 ab, Ch 3 a or Ch 3 x, and either Ch 1 ab, Ch 41 ab, or Ch 21 ab, and instructor’s permission.
Ch 10 ab is a weekly seminar by a member of the chemistry department on a topic of current research; the topic will be presented at an informal, introductory level. Ch 10 c is a research-oriented laboratory course, which will be supervised by a chemistry faculty member. Weekly class meetings will provide a forum for participants to discuss their research projects. Graded pass/fail.
Instructor: Hoelz
Ch 11. Biochemistry Laboratory.9 units (1-5-3); , 2022-23.Prerequisites: Ch/Bi 110 ab, Bi 8, or with permission of instructor.
The course will focus on techniques used in modern biochemistry laboratories. Students will learn how to express recombinant proteins in bacteria and purify them with various chromatography techniques. Purified proteins will be characterized by various in vitro assays.
Not offered 2022-23.
Instructor: Hoelz
BMB/Ch 230. Macromolecular Structure Determination with Modern X-ray Crystallography Methods.12 units (2-4-6); third term, 2022-23.Prerequisites: Consent of instructor.
Advanced course in macromolecular crystallography integrating lecture and laboratory treatment of diffraction theory, crystallization (proteins, nucleic acids and macromolecular complexes), crystal characterization, X-ray sources and optics, crystal freezing, X-ray diffraction data collection (in-house and synchrotron), data reduction, multiple isomorphous replacement, single- and multi-wavelength anomalous diffraction phasing techniques, molecular replacement, electron density interpretation, structure refinement, structure validation, coordinate deposition and structure presentation. In the laboratory component, one or more proteins will be crystallized and the structure(s) determined by several methods, in parallel with lectures on the theory and discussions of the techniques.
Instructor: Hoelz
BMB/Bi/Ch 174. Advanced Topics in Biochemistry and Biophysics.6 units (3-0-3); first term, 2019-20.Prerequisites: Bi/Ch 110 or equivalent.
Discussion of research fields in biochemistry and molecular biophysics at Caltech.
Instructors: Clemons, Hoelz, Shan and various guest lecturers
BMB/Ch 230. Macromolecular Structure Determination with Modern X-ray Crystallography Methods.12 units (2-4-6); third term, 2019-20.Prerequisites: Consent of instructor.
Advanced course in macromolecular crystallography integrating lecture and laboratory treatment of diffraction theory, crystallization (proteins, nucleic acids and macromolecular complexes), crystal characterization, X-ray sources and optics, crystal freezing, X-ray diffraction data collection (in-house and synchrotron), data reduction, multiple isomorphous replacement, single- and multi-wavelength anomalous diffraction phasing techniques, molecular replacement, electron density interpretation, structure refinement, structure validation, coordinate deposition and structure presentation. In the laboratory component, one or more proteins will be crystallized and the structure(s) determined by several methods, in parallel with lectures on the theory and discussions of the techniques
Instructor: Hoelz
