Protein Crystallographer – Fragments Discovery (Hybrid)

PE Global; Bracknell; Hybrid; GBP 39,316 - 52,362; Full time

Job summary

PE Global is currently recruiting for a Protein Crystallographer on a 12-month contract based in Bracknell. This hybrid role is ideal for an experienced structural biologist with a background in protein crystallography and fragment-based ligand discovery (FBLD).

The position requires hands-on expertise in crystallography and familiarity with PHENIX and BUSTER software. The successful candidate will engage in cutting-edge research while working closely with scientific partners to advance crystallography methods.

Qualifications

• PhD in Structural Biology, Biochemistry, or a related discipline.
• Significant hands-on experience in protein crystallography.
• Strong expertise with PHENIX and BUSTER software.

Responsibilities

• Utilise crystallography software to model and refine outputs.
• Coordinate X-ray data collection activities using resources.
• Design and analyse fragment screening experiments using X-ray crystallography.
• Collaborate with scientific partners to develop crystallography methods.
• Process large volumes of crystallographic datasets in parallel.
• Contribute to the improvement of structural biology workflows.

Skills

Protein crystallography

Fragment-based ligand discovery (FBLD)

PHENIX software

BUSTER software

Scripting crystallography workflows

High-Performance Computing (HPC)

Education

PhD in Structural Biology or related discipline

Tools

Crystallography software

Job description

PE Global is currently recruiting for a Protein Crystallographer on a 12-month contract based in Bracknell. This hybrid role is ideal for an experienced structural biologist with a background in protein crystallography and fragment-based ligand discovery (FBLD).

The position requires hands-on expertise in crystallography and familiarity with PHENIX and BUSTER software. The successful candidate will engage in cutting-edge research while working closely with scientific partners to advance crystallography methods.